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Mycobacteriophage endolysins: Diverse and modular enzymes with multiple catalytic activities

Payne, KM and Hatfull, GF (2012) Mycobacteriophage endolysins: Diverse and modular enzymes with multiple catalytic activities. PLoS ONE, 7 (3).

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The mycobacterial cell wall presents significant challenges to mycobacteriophages - viruses that infect mycobacterial hosts - because of its unusual structure containing a mycolic acid-rich mycobacterial outer membrane attached to an arabinogalactan layer that is in turn linked to the peptidoglycan. Although little is known about how mycobacteriophages circumvent these barriers during the process of infection, destroying it for lysis at the end of their lytic cycles requires an unusual set of functions. These include Lysin B proteins that cleave the linkage of mycolic acids to the arabinogalactan layer, chaperones required for endolysin delivery to peptidoglycan, holins that regulate lysis timing, and the endolysins (Lysin As) that hydrolyze peptidoglycan. Because mycobacterial peptidoglycan contains atypical features including 3→3 interpeptide linkages, it is not surprising that the mycobacteriophage endolysins also have non-canonical features. We present here a bioinformatic dissection of these lysins and show that they are highly diverse and extensively modular, with an impressive number of domain organizations. Most contain three domains with a novel N-terminal predicted peptidase, a centrally located amidase, muramidase, or transglycosylase, and a C-terminal putative cell wall binding domain. © 2012 Payne, Hatfull.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Payne, KMkim.payne@pitt.eduKMC830000-0001-8427-2465
Hatfull, GFgfh@pitt.eduGFH
ContributionContributors NameEmailPitt UsernameORCID
Date: 28 March 2012
Date Type: Publication
Journal or Publication Title: PLoS ONE
Volume: 7
Number: 3
DOI or Unique Handle: 10.1371/journal.pone.0034052
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
Other ID: NLM PMC3314691
PubMed Central ID: PMC3314691
PubMed ID: 22470512
Date Deposited: 03 Aug 2012 15:42
Last Modified: 06 Jan 2023 11:55


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