Pseudopeptidoglycan
Pseudopeptidoglycan (also known as pseudomurein[1]) is a major cell wall component of some Archaea that differs from bacterial peptidoglycan in chemical structure, but resembles bacterial peptidoglycan in function and physical structure. The basic components are N-acetylglucosamine and N-acetyltalosaminuronic acid (bacterial peptidoglycan containing N-acetylmuramic acid instead), which are linked by β-1,3-glycosidic bonds.
Lysozyme, a host defense mechanism present in human secretions (e.g. saliva and tears) breaks β-1,4-glycosidic bonds to degrade peptidoglycan; however because pseudopeptidoglycan has β-1,3-glycosidic bonds, lysozyme is ineffective.
Pseudomurein can be degraded by pseudomurein endoisopeptidase found in two prophages.[2]
See also
References
- ^ White, David. (1995) The Physiology and Biochemistry of Prokaryotes, pages 6, 12-21. (Oxford: Oxford University Press). ISBN 0-19-508439-X.
- ^ Visweswaran, Ganesh Ram R.; Dijkstra, Bauke W.; Kok, Jan (2010). "Two Major Archaeal Pseudomurein Endoisopeptidases: PeiW and PeiP". Archaea. 2010: 1–4. doi:10.1155/2010/480492. PMC 2989375. PMID 21113291.
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