Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase | Academic Article individual record
abstract

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 alpha/beta 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 DeltalysB 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.

author list (cited authors)
Payne, K., Sun, Q., Sacchettini, J., & Hatfull, G. F.
publication date
2009
publisher
Wiley Publisher
published in
keywords
  • Mycobacterium Smegmatis
  • Esterases
  • Viral Proteins
  • Peptidoglycan
  • Protein Structure, Tertiary
  • Galactans
  • Models, Molecular
  • Mycobacteriophages
  • Lipolysis
  • Mycolic Acids
  • Hydrolysis
altmetric score

6.0

citation count

80