Literature DB >> 16820517

The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain.

David M Donovan1, Juli Foster-Frey, Shengli Dong, Geneviève M Rousseau, Sylvain Moineau, David G Pritchard.   

Abstract

The Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. Truncations and point mutations indicated that the Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity.

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Year:  2006        PMID: 16820517      PMCID: PMC1489305          DOI: 10.1128/AEM.03065-05

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  22 in total

1.  SH3 domains in prokaryotes.

Authors:  J C Whisstock; A M Lesk
Journal:  Trends Biochem Sci       Date:  1999-04       Impact factor: 13.807

Review 2.  Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases.

Authors:  Daniel J Rigden; Mark J Jedrzejas; Michael Y Galperin
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3.  Old dogma, new tricks--21st Century phage therapy.

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5.  Antimicrobial susceptibility of Staphylococcus aureus isolated from bovine mastitis in Europe and the United States.

Authors:  A P De Oliveira; J L Watts; S A Salmon; F M Aarestrup
Journal:  J Dairy Sci       Date:  2000-04       Impact factor: 4.034

Review 6.  Engineering disease resistant cattle.

Authors:  David M Donovan; David E Kerr; Robert J Wall
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Review 7.  Changing patterns of infectious disease.

Authors:  M L Cohen
Journal:  Nature       Date:  2000-08-17       Impact factor: 49.962

8.  Discrimination of virulent and avirulent Streptococcus suis capsular type 2 isolates from different geographical origins.

Authors:  S Quessy; J D Dubreuil; M Caya; R Higgins
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9.  Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.

Authors:  Carine Huard; Guy Miranda; Françoise Wessner; Alexander Bolotin; Jonathan Hansen; Simon J Foster; Marie-Pierre Chapot-Chartier
Journal:  Microbiology       Date:  2003-03       Impact factor: 2.777

Review 10.  Mammary expression of new genes to combat mastitis.

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  31 in total

1.  Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site.

Authors:  Igor Abaev; Juli Foster-Frey; Olga Korobova; Nina Shishkova; Natalia Kiseleva; Pavel Kopylov; Sergey Pryamchuk; Mathias Schmelcher; Stephen C Becker; David M Donovan
Journal:  Appl Microbiol Biotechnol       Date:  2012-07-10       Impact factor: 4.813

2.  Biology and genome sequence of Streptococcus mutans phage M102AD.

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Journal:  Appl Environ Microbiol       Date:  2012-01-27       Impact factor: 4.792

3.  Endopeptidase and glycosidase activities of the bacteriophage B30 lysin.

Authors:  John R Baker; Chengbao Liu; Shengli Dong; David G Pritchard
Journal:  Appl Environ Microbiol       Date:  2006-10       Impact factor: 4.792

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5.  Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins.

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Review 6.  Recombinant Endolysins as Potential Therapeutics against Antibiotic-Resistant Staphylococcus aureus: Current Status of Research and Novel Delivery Strategies.

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Journal:  Clin Microbiol Rev       Date:  2017-11-29       Impact factor: 26.132

7.  LytN, a murein hydrolase in the cross-wall compartment of Staphylococcus aureus, is involved in proper bacterial growth and envelope assembly.

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8.  Molecular aspects and comparative genomics of bacteriophage endolysins.

Authors:  Hugo Oliveira; Luís D R Melo; Sílvio B Santos; Franklin L Nóbrega; Eugénio C Ferreira; Nuno Cerca; Joana Azeredo; Leon D Kluskens
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9.  SipA is required for pilus formation in Streptococcus pyogenes serotype M3.

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Journal:  Structure       Date:  2009-02-13       Impact factor: 5.006

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