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Pesquisa : D08.811.277.656.300.480.452 [Categoria DeCS]
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[PMID]:27943001
[Au] Autor:Raulinaitis V; Tossavainen H; Aitio O; Seppala R; Permi P
[Ad] Endereço:Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.
[Ti] Título:H, C and N resonance assignments of the new lysostaphin family endopeptidase catalytic domain from Staphylococcus aureus.
[So] Source:Biomol NMR Assign;11(1):69-73, 2017 Apr.
[Is] ISSN:1874-270X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Lysostaphin family endopeptidases, produced by Staphylococcus genus, are zinc-dependent enzymes that cleave pentaglycine bridges of cell wall peptidoglycan. They act as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Consequently, these enzymes are compelling targets for new drugs as well as are potential antimicrobial agents themselves against Staphylococcus pathogens, which depend on cell wall to retain their immunity against antibiotics. The rapid spread of methicillin and vancomycin-resistant Staphylococcus aureus strains draws demand for new therapeutic approaches. S. aureus gene sa0205 was found to be implicated in resistance to vancomycin and synthesis of the bacteria cell wall. The gene encodes for a catalytic domain of a lysostaphin-type endopeptidase. We aim to obtain the structure of the Sa0205 catalytic domain, the first solution structure of the catalytic domain of the lysostaphin family enzymes. In addition, we are to investigate the apparent binding of the second zinc ion, which has not been previously reported for the enzyme group. Herein, we present the backbone and side chain resonance assignments of Sa0205 endopeptidase catalytic domain in its one and two zinc-bound forms.
[Mh] Termos MeSH primário: Domínio Catalítico
Lisostafina/química
Ressonância Magnética Nuclear Biomolecular
Staphylococcus aureus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Lisostafina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1007/s12104-016-9722-7


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[PMID]:27699884
[Au] Autor:Xing M; Simmonds RS; Timkovich R
[Ad] Endereço:Department of Chemistry, University of Alabama, Tuscaloosa, Alabama, 35487.
[Ti] Título:Solution structure of the Cys74 to Ala74 mutant of the recombinant catalytic domain of Zoocin A.
[So] Source:Proteins;85(1):177-181, 2017 Jan.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zoocin A is a Zn-metallopeptidase secreted by Streptococcus zooepidemicus strain 4881. Its catalytic domain is responsible for cleaving the D-alanyl-L-alanine peptide bond in streptococcal peptidoglycan. The solution NMR structure of the Cys74 to Ala74 mutant of the recombinant catalytic domain (rCAT C74A) has been determined. With a previous structure determination for the recombinant target recognition domain (rTRD), this completes the 3D structure of zoocin A. While the structure of rCAT C74A resembles those of the catalytic domains of lysostaphin and LytM, the substrate binding groove is wider and no tyrosine residue was observed in the active site. Proteins 2016; 85:177-181. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Alanina/química
Proteínas de Bactérias/química
Bacteriocinas/química
Cisteína/química
Mutação
Streptococcus equi/química
[Mh] Termos MeSH secundário: Alanina/metabolismo
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Bacteriocinas/genética
Bacteriocinas/metabolismo
Domínio Catalítico
Clonagem Molecular
Cisteína/metabolismo
Endopeptidases/química
Endopeptidases/genética
Endopeptidases/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Lisostafina/química
Lisostafina/metabolismo
Modelos Moleculares
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Streptococcus equi/enzimologia
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacteriocins); 0 (Recombinant Proteins); EC 3.4.- (Endopeptidases); EC 3.4.24.75 (Lysostaphin); EC 3.4.99.- (LytM protein, Staphylococcus aureus); K848JZ4886 (Cysteine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161005
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25178


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[PMID]:27363205
[Au] Autor:Lu H; Zhangi Y; Huang Q
[Ti] Título:[Site-specific PEGylation of recombinant lysostaphin].
[So] Source:Sheng Wu Gong Cheng Xue Bao;32(1):127-34, 2016 Jan.
[Is] ISSN:1000-3061
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Lysostaphin (Lysn) is an antibacterial metalloendopeptidase that cleaves the pentaglycin bridges in the cell wall of Staphylococci. Although many studies have demonstrated its high activity in vitro, the medical application of Lysn has been hampered by its short half-life in vivo. In order to enhance its stability in vivo without significantly suppressing the enzymatic activity, we designed and tested eight single cysteine substitutions in Lysn for covalent attachment of polyethylene glycol chains (PEGylation). The purified mutants, fully reduced by Dithiothreitol (DTT), were treated with mPEG-MAL(20 kDa). The PEG modification efficiency was above 70% as determined by reverse-phase high-pressure liquid chromatography (HPLC) analysis. The PEG-Lysn proteins were further purified by cation exchange chromatography (MacroCap SP), reaching at least 95% purity. The activities of the PEG-Lysn proteins were determined by the turbidity and minimum inhibitory concentration (MIC) assays. We found that the PEGylated V240C and T244C mutants retained about 50% of the original antibacterial activity of Lysn. Overall, this study will help develop highly stable and active PEG-Lysn to treat systemic S. aureus infections.
[Mh] Termos MeSH primário: Lisostafina/química
Polietilenoglicóis/química
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Proteínas Recombinantes/química
Staphylococcus aureus
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Recombinant Proteins); 30IQX730WE (Polyethylene Glycols); EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:160701
[Lr] Data última revisão:
160701
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160702
[St] Status:MEDLINE


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[PMID]:27351490
[Au] Autor:Jagielska E; Chojnacka O; Sabala I
[Ad] Endereço:International Institute of Molecular and Cell Biology in Warsaw , Warsaw, Poland .
[Ti] Título:LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.
[So] Source:Microb Drug Resist;22(6):461-9, 2016 Sep.
[Is] ISSN:1931-8448
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Proteínas de Bactérias/metabolismo
Endopeptidases/metabolismo
Lisostafina/metabolismo
Proteínas Recombinantes de Fusão/biossíntese
Staphylococcus aureus/metabolismo
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/farmacologia
Parede Celular/química
Parede Celular/efeitos dos fármacos
Parede Celular/metabolismo
Endopeptidases/genética
Endopeptidases/farmacologia
Expressão Gênica
Lisostafina/farmacologia
Testes de Sensibilidade Microbiana
Mutação
Domínios Proteicos
Engenharia de Proteínas
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/farmacologia
Staphylococcus aureus/efeitos dos fármacos
Staphylococcus aureus/genética
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Recombinant Fusion Proteins); EC 3.4.- (Endopeptidases); EC 3.4.24.75 (Lysostaphin); EC 3.4.99.- (LytM protein, Staphylococcus aureus)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170419
[Lr] Data última revisão:
170419
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160629
[St] Status:MEDLINE
[do] DOI:10.1089/mdr.2016.0053


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[PMID]:27297900
[Au] Autor:Boksha IS; Lavrova NV; Grishin AV; Demidenko AV; Lyashchuk AM; Galushkina ZM; Ovchinnikov RS; Umyarov AM; Avetisian LR; Chernukha MIu; Shaginian IA; Lunin VG; Karyagina AS
[Ad] Endereço:N. F. Gamaleya Federal Research Centre for Epidemiology and Microbiology, Ministry of Health of the Russian Federation, Moscow, 123098, Russia. boksha_irina@mail.ru.
[Ti] Título:Staphylococcus simulans Recombinant Lysostaphin: Production, Purification, and Determination of Antistaphylococcal Activity.
[So] Source:Biochemistry (Mosc);81(5):502-10, 2016 May.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Staphylococcus simulans lysostaphin is an endopeptidase lysing staphylococcus cell walls by cleaving pentaglycine cross-bridges in their peptidoglycan. A synthetic gene encoding S. simulans lysostaphin was cloned in Escherichia coli cells, and producer strains were designed. The level of produced biologically active lysostaphin comprised 6-30% of total E. coli cell protein (depending on E. coli M15 or BL21 producer) under batch cultivation conditions. New methods were developed for purification of lysostaphin without affinity domains and for testing its enzymatic activity. As judged by PAGE, the purified recombinant lysostaphin is of >97% purity. The produced lysostaphin lysed cells of Staphylococcus aureus and Staphylococcus haemolyticus clinical isolates. In vitro activity and general biochemical properties of purified recombinant lysostaphin produced by M15 or BL21 E. coli strains were identical to those of recombinant lysostaphin supplied by Sigma-Aldrich (USA) and used as reference in other known studies. The prepared recombinant lysostaphin represents a potential product for development of enzymatic preparation for medicine and veterinary due to the simple purification scheme enabling production of the enzyme of high purity and antistaphylococcal activity.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Lisostafina/farmacologia
Staphylococcus/genética
[Mh] Termos MeSH secundário: Antibacterianos/biossíntese
Antibacterianos/isolamento & purificação
Proteínas de Bactérias/metabolismo
Biomassa
Clonagem Molecular
Testes de Sensibilidade a Antimicrobianos por Disco-Difusão
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Escherichia coli/metabolismo
Lisostafina/biossíntese
Lisostafina/isolamento & purificação
Peptidoglicano/metabolismo
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/farmacologia
Staphylococcus/efeitos dos fármacos
Staphylococcus aureus/efeitos dos fármacos
Staphylococcus haemolyticus/efeitos dos fármacos
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Peptidoglycan); 0 (Recombinant Proteins); EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170112
[Lr] Data última revisão:
170112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160615
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297916050072


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[PMID]:27168405
[Au] Autor:Filatova LY; Donovan DM; Ishnazarova NT; Foster-Frey JA; Becker SC; Pugachev VG; Balabushevich NG; Dmitrieva NF; Klyachko NL
[Ad] Endereço:Department of Chemical Enzymology, Faculty of Chemistry, M.V. Lomonosov Moscow State University, Moscow, Russia. luboff.filatova@gmail.com.
[Ti] Título:A Chimeric LysK-Lysostaphin Fusion Enzyme Lysing Staphylococcus aureus Cells: a Study of Both Kinetics of Inactivation and Specifics of Interaction with Anionic Polymers.
[So] Source:Appl Biochem Biotechnol;180(3):544-557, 2016 Oct.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A staphylolytic fusion protein (chimeric enzyme K-L) was created, harboring three unique lytic activities composed of the LysK CHAP endopeptidase, and amidase domains, and the lysostaphin glycyl-glycine endopeptidase domain. To assess the potential of possible therapeutic applications, the kinetic behavior of chimeric enzyme K-L was investigated. As a protein antimicrobial, with potential antigenic properties, the biophysical effect of including chimeric enzyme K-L in anionic polymer matrices that might help reduce the immunogenicity of the enzyme was tested. Chimeric enzyme K-L reveals a high lytic activity under the following optimal ( ) conditions: pH 6.0-10.0, t 20-30 °C, NaCl 400-800 mM. At the working temperature of 37 °C, chimeric enzyme K-L is inactivated by a monomolecular mechanism and possesses a high half-inactivation time of 12.7 ± 3.0 h. At storage temperatures of 22 and 4 °C, a complex mechanism (combination of monomolecular and bimolecular mechanisms) is involved in the chimeric enzyme K-L inactivation. The optimal storage conditions under which the enzyme retains 100 % activity after 140 days of incubation (4 °C, the enzyme concentration of 0.8 mg/mL, pH 6.0 or 7.5) were established. Chimeric enzyme K-L is included in complexes with block-copolymers of poly-L-glutamic acid and polyethylene glycol, while the enzyme activity and stability are retained, thus suggesting methods to improve the application of this fusion as an effective antimicrobial agent.
[Mh] Termos MeSH primário: Ânions/farmacologia
Proteínas de Bactérias/farmacologia
Bacteriólise/efeitos dos fármacos
Lisostafina/farmacologia
Polímeros/farmacologia
Proteínas Recombinantes de Fusão/farmacologia
Staphylococcus aureus/citologia
[Mh] Termos MeSH secundário: Ativação Enzimática/efeitos dos fármacos
Estabilidade Enzimática/efeitos dos fármacos
Concentração de Íons de Hidrogênio
Cinética
Tamanho da Partícula
Cloreto de Sódio/farmacologia
Staphylococcus aureus/efeitos dos fármacos
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anions); 0 (Bacterial Proteins); 0 (Polymers); 0 (Recombinant Fusion Proteins); 451W47IQ8X (Sodium Chloride); EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160512
[St] Status:MEDLINE


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[PMID]:27058327
[Au] Autor:Sahin F; Kiyan M; Karasartova D; Çalgin MK; Akhter S; Türegün Atasoy B
[Ad] Endereço:Ankara University Faculty of Medicine, Department of Medical Microbiology, Ankara, Turkey. fsahin29@hotmail.com.
[Ti] Título:[A new method for the disruption of cell walls of gram-positive bacteria and mycobacteria on the point of nucleic acid extraction: sand method].
[Ti] Título:Nükleik asit ekstraksiyonunda kullanilmak üzere, gram-pozitif bakteriler ve mikobakterilerin hücre duvarlarinin ortadan kaldirilmasinda yeni bir yöntem: Kum yöntemi..
[So] Source:Mikrobiyol Bul;50(1):34-43, 2016 Jan.
[Is] ISSN:0374-9096
[Cp] País de publicação:Turkey
[La] Idioma:tur
[Ab] Resumo:Nowadays molecular methods are widely used in the rapid diagnosis of infectious agents. Polymerase chain reaction (PCR) is the most preferred method for this purpose. Obtaining sufficient and pure DNA or RNA is important for the PCR. Different DNA extraction protocols such as phenol-chloroform, proteinase K, glass beads and boiling have been used successfully for DNA isolation from gram-negative bacteria. However since gram-positive bacteria have a thicker layer of peptidoglycan and mycobacteria have complex glycolipids in their cell walls, for the isolation of DNA or RNA from these microorganisms, the complex cell wall structure must be eliminated. For this purpose, the bacterial cell wall must be completely or partially removed forming sferoblast using lysostaphin in the Staphylococcus genus as gram-positive bacteria and using a chemical like cetyltrimethyl ammonium bromide for the Mycobacterium genus. In this study, we planned to use sand particles for the mechanical elimination of the cell wall without any need for chemicals and we called this procedure as "sand method". For the purpose of DNA extraction, the fine-grained sand was washed with ddH(2)O without losing small particles and then sterilized by autoclaving. For the purpose of RNA extraction; the sand was washed with ddH(2)O, incubated for 30 minutes with 10% HCl, and then autoclaved. A methicillin-resistant Staphylococcus aureus (MRSA) strain previously isolated and identified from a clinical specimen was mixed in 100 µl Tris-EDTA buffer with 100 mg sand. The mixture of bacteria and sand was vortexed at the maximum speed for 5 minutes. The MRSA-sand mix was treated with proteinase K and phenol-chloroform, and ethanol precipitation protocol was then followed for obtaining DNA. For comparison of the sand method with the other methods, the same amount of bacteria used in the sand method was incubated for one hour with lysostaphin, and then the proteinase K DNA extraction method were completed in the same way used in the sand method. For obtaining RNA from M.tuberculosis H37Rv ATCC 25618, M.tuberculosis H37Ra ATCC 25177 and M.tuberculosis H37Rv Pasteur Institute RSKK 598 standard strains, bacteria were dissolved in 20 µl Tris-EDTA buffer with 100 mg sand. The mixture of bacteria and sand was vortexed at the maximum speed for 5 minutes. After that, the classic RNA extraction protocol using guanidinium thiocyanate-phenol-chloroform (GTPC) was completed. To investigate the usefulness of the obtained DNA, a PCR was performed with specific primers for staphylokinase and enterotoxin genes that were shown in the genome of the chosen MRSA strains from our previous studies. To investigate the usefulness of the obtained RNA from the sand method; first cDNA synthesis is completed. The PCR efficiency was then tested using primers specific to the efflux pump genes of M.tuberculosis including Rv1410c, Rv2333c, and DrrA genes. To compare the effect of the sand method, GTPC protocol was applied in the same amount of mycobacteria without the sand treatment. The DNA obtained from MRSA with the application of lysostaphin and the DNA obtained from MRSA by the sand method were run in agarose gel electrophoresis. The amount and purity of DNAs were measured with a spectrophotometer. The same amount and purity of the DNAs were approximately the same in both of the extraction methods. The existence of non-inhibitors of DNA in the sand method was shown with the PCR, which have worked efficiently with the DNAs obtained from the sand method. RNA was obtained efficiently from the Mycobacterium strains by the sand method, but no RNA could be obtained from the mycobacteria with the other methods. It was shown that the RNA obtained using the sand method worked effectively in both cDNA synthesis and PCR in which synthesized cDNA was used. The sand method described in the study worked effectively to obtain sufficient amount of pure DNA and RNA from the bacteria containing rigid cell walls that are difficult to obtain the nucleotide. It was concluded that, using the sand method instead of relatively expensive lysostaphin or other chemicals, has important advantages such as decreasing the cost and the shortening of the DNA extraction period.
[Mh] Termos MeSH primário: DNA Bacteriano/isolamento & purificação
Bactérias Gram-Positivas/genética
Mycobacterium/genética
RNA Bacteriano/isolamento & purificação
[Mh] Termos MeSH secundário: Parede Celular/química
Parede Celular/ultraestrutura
Primers do DNA/química
DNA Bacteriano/química
Bactérias Gram-Positivas/química
Lisostafina
Mycobacterium/química
Reação em Cadeia da Polimerase/normas
RNA Bacteriano/química
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Primers); 0 (DNA, Bacterial); 0 (RNA, Bacterial); EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160409
[Lr] Data última revisão:
160409
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160409
[St] Status:MEDLINE


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[PMID]:27040789
[Au] Autor:Hoernig KJ; Donovan DM; Pithua P; Williams F; Middleton JR
[Ad] Endereço:Department of Veterinary Medicine and Surgery, University of Missouri, Columbia 65211.
[Ti] Título:Evaluation of a lysostaphin-fusion protein as a dry-cow therapy for Staphylococcus aureus mastitis in dairy cattle.
[So] Source:J Dairy Sci;99(6):4638-4646, 2016 Jun.
[Is] ISSN:1525-3198
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study evaluated the efficacy of a recombinant lysostaphin fused to a protein transduction domain (rLYS-PTD) as a dry-cow therapy for the treatment of experimentally induced chronic, subclinical Staphylococcus aureus mastitis. Twenty-two Holstein dairy cows were experimentally infected with Staph. aureus in a single pair of diagonal mammary quarters approximately 45d before dry off. Staphylococcus aureus-infected mammary quarters of cows were randomly assigned to 1 of 2 treatment groups at dry off: (1) 279mg of rLYS-PTD in 50mL of vehicle (n=11 cows; 22 quarters) or (2) 50mL of vehicle solution (n=11 cows; 22 quarters) by intramammary infusion. All cows were followed for 30d postpartum to determine cure rates using bacteriologic culture, somatic cell counts, and clinical mastitis scores. No cures were recorded in either the treatment or control groups. Milk somatic cell count, bacterial colony counts, and mastitis scores did not significantly differ between treatment groups. In conclusion, rLYS-PTD was not an effective dry-cow therapeutic for chronic, subclinical Staph. aureus mastitis at the tested dose and formulation.
[Mh] Termos MeSH primário: Antibacterianos/uso terapêutico
Anti-Infecciosos Locais/uso terapêutico
Lisostafina/uso terapêutico
Mastite Bovina/tratamento farmacológico
Infecções Estafilocócicas/veterinária
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Bovinos
Feminino
Glândulas Mamárias Animais/efeitos dos fármacos
Glândulas Mamárias Animais/microbiologia
Mastite Bovina/microbiologia
Infecções Estafilocócicas/tratamento farmacológico
Infecções Estafilocócicas/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Anti-Infective Agents, Local); EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160405
[St] Status:MEDLINE


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[PMID]:26999597
[Au] Autor:Ceotto-Vigoder H; Marques SL; Santos IN; Alves MD; Barrias ES; Potter A; Alviano DS; Bastos MC
[Ad] Endereço:Departamento de Microbiologia Geral, Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
[Ti] Título:Nisin and lysostaphin activity against preformed biofilm of Staphylococcus aureus involved in bovine mastitis.
[So] Source:J Appl Microbiol;121(1):101-14, 2016 Jul.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: The biofilm produced by Staphylococcus aureus isolates involved in clinical or subclinical bovine mastitis and the activity of nisin and lysostaphin against the preformed biofilm produced by these strains were investigated. METHODS AND RESULTS: Eighteen strains were tested and all produced biofilm. Eight strains with distinct biofilm composition were selected for the antimicrobial activity assays. The minimal inhibitory concentration of each bacteriocin was determined against the planktonic cells and ranged from 15·6 to 500 µg ml(-1) for nisin, and from 3·9 to 50 µg ml(-1) , for lysostaphin. Lysostaphin treatment (0·4 µg ml(-1) ) for 4 h caused a strong Staph. aureus 4181 biofilm detachment and death of the majority of the sessile cells, while nisin treatment (100 µg ml(-1) ) for the same time caused only a great reduction in cell viability. Additionally, combination of both bacteriocins for 4 h resulted in significant death of the sessile cells but no biofilm detachment. CONCLUSIONS: The treatment with lysostaphin alone or in combination with nisin was effective in killing most biofilm sessile cells. SIGNIFICANCE AND IMPACT OF THE STUDY: The action of lysostaphin, either alone or in combination with nisin, against established staphylococcal biofilm may represent an alternative to bovine mastitis control. However, the duration of the treatment should be considered for its application so that the best effectiveness can be achieved.
[Mh] Termos MeSH primário: Biofilmes/efeitos dos fármacos
Lisostafina/farmacologia
Mastite Bovina/tratamento farmacológico
Nisina/farmacologia
Infecções Estafilocócicas/tratamento farmacológico
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Antibacterianos/farmacologia
Bovinos
Sobrevivência Celular/efeitos dos fármacos
Feminino
Lisostafina/uso terapêutico
Testes de Sensibilidade Microbiana/métodos
Nisina/uso terapêutico
Plâncton/efeitos dos fármacos
Staphylococcus aureus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 1414-45-5 (Nisin); EC 3.4.24.75 (Lysostaphin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160322
[St] Status:MEDLINE
[do] DOI:10.1111/jam.13136


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[PMID]:26678532
[Au] Autor:Drilling AJ; Cooksley C; Chan C; Wormald PJ; Vreugde S
[Ad] Endereço:Department of Surgery-Otolaryngology Head and Neck Surgery, University of Adelaide, Adelaide, Australia.
[Ti] Título:Fighting sinus-derived Staphylococcus aureus biofilms in vitro with a bacteriophage-derived muralytic enzyme.
[So] Source:Int Forum Allergy Rhinol;6(4):349-55, 2016 Apr.
[Is] ISSN:2042-6984
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Staphylococcus aureus biofilms are a nidus for exacerbation of infectious conditions including chronic rhinosinusitis (CRS). Resistance of biofilms to current therapeutics stresses the need for the development of novel anti-biofilm strategies. The chimeric muralytic enzyme P128 was specifically engineered to target Staphylococcal sp. by combining the cell wall binding domain of lysostaphin and the peptidoglycan-degrading murein hydrolase derived from phage K. This study assessed the anti-biofilm activity of P128 against sinus-derived S. aureus. METHODS: Biofilms from S. aureus ATCC 25923 and 3 sinus-derived methicillin-sensitive and methicillin-resistant CRS clinical isolates were grown for 48 hours and treated with various concentrations of P128 (0 to 100 µg/mL) for 2 and 24 hours, using the minimum biofilm eradication concentration (MBEC) assay and Alamar Blue (AB) assay. Biofilm present on the MBEC pegs was stained with LIVE/DEAD BacLight stain, imaged using confocal scanning laser microscopy and biomass determined by COMSTAT2 computation. In the AB assay, biofilm was measured by assessing the cell viability. Results were assessed using a Kruskal-Wallis test, with a Wilcoxon post hoc test and Bonferroni correction. RESULTS: Both the MBEC and AB assay indicated that P128 was effective against in vitro S. aureus biofilms with significant reductions in biofilm of up to 95.5% at concentrations ≥12.5 µg/mL for all tested strains. CONCLUSION: The engineered chimeric endolysin P128 was observed to be an effective anti-biofilm agent against S. aureus. Further study will proceed into the appropriate application of P128 to ensure both an economically and clinically feasible preparation.
[Mh] Termos MeSH primário: Biofilmes/efeitos dos fármacos
Proteínas Recombinantes de Fusão/farmacologia
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Bacteriófagos/enzimologia
Lisostafina
N-Acetil-Muramil-L-Alanina Amidase
Seios Paranasais/microbiologia
Staphylococcus aureus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (P128 antistaphylococcal chimeric protein); 0 (Recombinant Fusion Proteins); EC 3.4.24.75 (Lysostaphin); EC 3.5.1.28 (N-Acetylmuramoyl-L-alanine Amidase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161231
[Lr] Data última revisão:
161231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151219
[St] Status:MEDLINE
[do] DOI:10.1002/alr.21680



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