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

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.

SUBMITTER: Kang D

PROVIDER: S-EPMC21464 | biostudies-literature | 1998 Aug

REPOSITORIES: biostudies-literature

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

Kang D D Liu G G Lundström A A Gelius E E Steiner H H

Proceedings of the National Academy of Sciences of the United States of America 19980801 17

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 a ...[more]

PMID: 9707603

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