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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Weiss, J. Search for Related Content PubMed Articles by Weiss, J. Related Collections Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 July 2003, Vol. 102, No. 2, pp. 419 Peptidoglycan recognition and neutrophil function Host responses and defense against invading micro-organisms depend on highly conserved innate immune recognition systems that react with conserved motifs found uniquely in microbes. The Toll-like receptors are related proteins mediating inflammatory responses in a wide variety of cells, each receptor triggered by a distinct subset of microbial products. Host peptidoglycan recognition proteins (PGRPs), by contrast, share the ability to bind bacterial cell wall peptidoglycan (fragments) but are expressed at different cellular and tissue sites, suggesting that each PGRP may link peptidoglycan recognition to distinct host responses (Werner et al, Proc Nat Acad Sci U S A. 2000;97:13772-13777; Liu et al, J Biol Chem. 2001;276:34686-34694). Genes encoding 4 different PGRPs have been identified in the human genome by homology to conserved insect PGRP domains (Liu et al). One, PGRP-S, is highly expressed in bone marrow and encodes an approximately 19-kDa protein present in neutrophils, cells that play an essential early role in host defense against many invading bacteria (Liu et al; Liu et al, J Biol Chem. 2000;275:24490-24499). To test the possible role of PGRP-S in host defense against bacterial infections, Dziarski and colleagues (page 689) have produced PGRP-S–deficient mice and, in so doing, demonstrate a role for PGRP-S in in vitro bacterial killing by neutrophils and in vivo clearance of intraperitoneal bacterial infection. The localization of PGRP-S in readily mobilized granules suggests not only a role in intracellular cytotoxicity after phagocytosis, as is shown, but also possible extracellular roles within neutrophil-rich inflammatory exudates. These studies reveal novel effector functions of mammalian PGRP-S and suggest that although while peptidoglycan recognition has been conserved within insect and mammalian orthologues, effector functions have changed to coordinate PGRP function with evolving organizations of host defense against bacteria. Jerrold Weiss University of Iowa CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Defect in neutrophil killing and increased susceptibility to infection with nonpathogenic gram-positive bacteria in peptidoglycan recognition protein-S (PGRP-S)–deficient mice Roman Dziarski, Kenneth A. Platt, Eva Gelius, Håkan Steiner, and Dipika Gupta Blood 2003 102: 689-697. [Abstract] [Full Text] [PDF] This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Weiss, J. Search for Related Content PubMed Articles by Weiss, J. Related Collections Related Article in Blood Online Social Bookmarking                   What's this?

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