Literature DB >> 9707603

A peptidoglycan recognition protein in innate immunity conserved from insects to humans.

D Kang1, G Liu, A Lundström, E Gelius, H Steiner.   

Abstract

Innate nonself recognition must rely on common structures of invading microbes. In a differential display screen for up-regulated immune genes in the moth Trichoplusia ni we have found mechanisms for recognition of bacterial cell wall fragments. One bacteria-induced gene encodes a protein that, after expression in the baculovirus system, was shown to be a peptidoglycan recognition protein (PGRP). It binds strongly to Gram-positive bacteria. We have also cloned the corresponding cDNA from mouse and human and shown this gene to be expressed in a variety of organs, notably organs of the immune system-i.e., bone marrow and spleen. In addition, purified recombinant murine PGRP was shown to possess peptidoglycan affinity. From our results and the sequence homology, we conclude that PGRP is a ubiquitous protein involved in innate immunity, conserved from insects to humans.

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Year:  1998        PMID: 9707603      PMCID: PMC21464          DOI: 10.1073/pnas.95.17.10078

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  25 in total

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5.  Structure and function of lipopolysaccharide binding protein.

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  110 in total

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Review 7.  Dissecting innate immunity by germline mutagenesis.

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