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Paired receptors are families of membrane proteins containing similar extracellular regions but differing in their potential for signaling with one type able to give inhibitory signals and the other activating. Inhibitory receptors could be good targets for pathogens to restrict immune responses against them. Here we suggest that activating members may have evolved to counterbalance pathogens utilizing the inhibitory pathway. Thus, if a pathogen utilizes any part of the inhibitory receptor to downregulate responses against itself, it may, because of similarities in structure, also bind the activating receptor and give an opposing signal. We evaluate recent structural data on SIRPalpha (signal regulatory protein) and LILRB1 (leukocyte immunoglobulin-like receptor subfamily B member 1) showing evidence of pathogen pressure in nonligand-binding regions of these receptors together with data on pathogen binding to PIRs (paired Ig-like receptors) to provide support for this theory.

Original publication

DOI

10.1016/j.immuni.2008.10.004

Type

Journal article

Journal

Immunity

Publication Date

14/11/2008

Volume

29

Pages

675 - 678

Keywords

Amino Acid Sequence, Animals, Antigens, Differentiation, Bacteria, Evolution, Molecular, Humans, Killer Cells, Natural, Ligands, Membrane Proteins, Molecular Sequence Data, Polymorphism, Genetic, Protein Binding, Receptors, Immunologic, Sequence Alignment, Viruses