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.
MeSH Terms
Amino Acid Sequence
Animals
Bacteria/immunology
Baculoviridae/genetics
Base Sequence
Conserved Sequence
Humans
Immunity/genetics
Insect Proteins/genetics,immunology,metabolism
Male
Mice
Molecular Sequence Data
Moths/genetics,immunology
Peptidoglycan/immunology,metabolism
Polymerase Chain Reaction
Protein Binding
Proteins/genetics,immunology,metabolism
RNA, Messenger/genetics,metabolism
Recombinant Proteins/genetics,immunology
Sequence Homology, Amino Acid
Tissue Distribution
Chemicals
Insect Proteins
Peptidoglycan
Proteins
RNA, Messenger
Recombinant Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kang D
Department of Microbiology, Stockholm University, S-106 91 Stockholm, Sweden.
Liu G
Lundström A
Gelius E
Steiner H
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