The Pseudokinase NIPI-4 Is a Novel Regulator of Antimicrobial Peptide Gene Expression

Citation metadata

Authors: Sid ahmed Labed, Shizue Omi, Martha Gut, Jonathan J. Ewbank and Nathalie Pujol
Date: Mar. 21, 2012
From: PLoS ONE(Vol. 7, Issue 3)
Publisher: Public Library of Science
Document Type: Article
Length: 7,224 words

Main content

Abstract :

Hosts have developed diverse mechanisms to counter the pathogens they face in their natural environment. Throughout the plant and animal kingdoms, the up-regulation of antimicrobial peptides is a common response to infection. In C. elegans, infection with the natural pathogen Drechmeria coniospora leads to rapid induction of antimicrobial peptide gene expression in the epidermis. Through a large genetic screen we have isolated many new mutants that are incapable of upregulating the antimicrobial peptide nlp-29 in response to infection (i.e. with a Nipi or 'no induction of peptide after infection' phenotype). More than half of the newly isolated Nipi mutants do not correspond to genes previously associated with the regulation of antimicrobial peptides. One of these, nipi-4, encodes a member of a nematode-specific kinase family. NIPI-4 is predicted to be catalytically inactive, thus to be a pseudokinase. It acts in the epidermis downstream of the PKC[partial differential] TPA-1, as a positive regulator of nlp antimicrobial peptide gene expression after infection. It also controls the constitutive expression of antimicrobial peptide genes of the cnc family that are targets of TGFß regulation. Our results open the way for a more detailed understanding of how host defense pathways can be molded by environmental pathogens.

Source Citation

Source Citation
Labed, Sid ahmed, et al. "The Pseudokinase NIPI-4 Is a Novel Regulator of Antimicrobial Peptide Gene Expression." PLoS ONE, vol. 7, no. 3, 21 Mar. 2012, p. e33887. Accessed 26 June 2022.

Gale Document Number: GALE|A477052757