| Identification of a bacterial inhibitor against g-type lysozyme. | |
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MedLine Citation:
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PMID: 20734102 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Lysozymes are antibacterial effectors of the innate immune system in animals that hydrolyze peptidoglycan. Bacteria have evolved protective mechanisms that contribute to lysozyme tolerance such as the production of lysozyme inhibitors, but only inhibitors of chicken (c-) and invertebrate (i-) type lysozyme have been identified. We here report the discovery of a novel Escherichia coli inhibitor specific for goose (g-) type lysozymes, which we designate PliG (periplasmic lysozyme inhibitor of g-type lysozyme). Although it does not inhibit c- or i-type lysozymes, PliG shares a structural sequence motif with the previously described PliI and MliC/PliC lysozyme inhibitor families, suggesting a common ancestry and mode of action. Deletion of pliG increased the sensitivity of E. coli to g-type lysozyme. The existence of inhibitors against all major types of animal lysozyme and their contribution to lysozyme tolerance suggest that lysozyme inhibitors may play a role in bacterial interactions with animal hosts. |
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Authors:
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L Vanderkelen; J M Van Herreweghe; K G A Vanoirbeek; G Baggerman; B Myrnes; P J Declerck; I W Nilsen; C W Michiels; L Callewaert |
Publication Detail:
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Type: Journal Article Date: 2010-08-25 |
Journal Detail:
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Title: Cellular and molecular life sciences : CMLS Volume: 68 ISSN: 1420-9071 ISO Abbreviation: Cell. Mol. Life Sci. Publication Date: 2011 Mar |
Date Detail:
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Created Date: 2011-02-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9705402 Medline TA: Cell Mol Life Sci Country: Switzerland |
Other Details:
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Languages: eng Pagination: 1053-64 Citation Subset: IM |
Affiliation:
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Laboratory of Food Microbiology and Leuven Food Science and Nutrition Research Centre (LFoRCe), Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, 3001, Leuven, Belgium. |
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