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Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase

Payne, K and Sun, Q and Sacchettini, J and Hatfull, GF (2009) Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase. Molecular Microbiology, 73 (3). 367 - 381. ISSN 0950-382X

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Mycobacteriophages encounter a unique problem among phages of Gram-positive bacteria, in that lysis must not only degrade the peptidoglycan layer but also circumvent a mycolic acid-rich outer membrane covalently attached to the arabinogalactan-peptidoglycan complex. Mycobacteriophages accomplish this by producing two lysis enzymes, Lysin A (LysA) that hydrolyses peptidoglycan, and Lysin B (LysB), a novel mycolylarabinogalactan esterase, that cleaves the mycolylarabinogalactan bond to release free mycolic acids. The D29 LysB structure shows an α/β hydrolase organization with a catalytic triad common to cutinases, but which contains an additional four-helix domain implicated in the binding of lipid substrates. Whereas LysA is essential for mycobacterial lysis, a Giles ΔlysB mutant mycobacteriophage is viable, but defective in the normal timing, progression and completion of host cell lysis. We propose that LysB facilitates lysis by compromising the integrity of the mycobacterial outer membrane linkage to the arabinogalactan-peptidoglycan layer. © 2009 The Authors. Journal compilation © 2009 Blackwell Publishing Ltd.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Payne, Kkim.payne@pitt.eduKMC830000-0001-8427-2465
Sun, Q
Sacchettini, J
Hatfull, GFgfh@pitt.eduGFH
Date: 1 August 2009
Date Type: Publication
Journal or Publication Title: Molecular Microbiology
Volume: 73
Number: 3
Page Range: 367 - 381
DOI or Unique Handle: 10.1111/j.1365-2958.2009.06775.x
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0950-382X
MeSH Headings: Esterases--genetics; Esterases--metabolism; Galactans--metabolism; Hydrolysis; Lipolysis; Models, Molecular; Mycobacteriophages--enzymology; Mycobacteriophages--genetics; Mycobacterium smegmatis--virology; Mycolic Acids--metabolism; Peptidoglycan--metabolism; Protein Structure, Tertiary; Viral Proteins--genetics; Viral Proteins--metabolism
Other ID: NLM NIHMS145624, NLM PMC2774421
PubMed Central ID: PMC2774421
PubMed ID: 19555454
Date Deposited: 05 Dec 2012 16:51
Last Modified: 06 Jan 2023 11:55


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