Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.

Peptidoglycan is an essential and specific component of the bacterial cell wall and therefore is an ideal recognition signature for the immune system. Peptidoglycan recognition proteins (PGRPs) are conserved from insects to mammals and able to bind PGN (non-catalytic PGRPs) and, in some cases, to ef...

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Autores principales:	Anna Zaidman-Rémy, Mickael Poidevin, Mireille Hervé, David P Welchman, Juan C Paredes, Carina Fahlander, Hakan Steiner, Dominique Mengin-Lecreulx, Bruno Lemaitre
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/34a45adc0e3245e6831bd0f56244a6f9
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spelling	oai:doaj.org-article:34a45adc0e3245e6831bd0f56244a6f92021-11-18T06:58:33ZDrosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.1932-620310.1371/journal.pone.0017231https://doaj.org/article/34a45adc0e3245e6831bd0f56244a6f92011-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21364998/?tool=EBIhttps://doaj.org/toc/1932-6203Peptidoglycan is an essential and specific component of the bacterial cell wall and therefore is an ideal recognition signature for the immune system. Peptidoglycan recognition proteins (PGRPs) are conserved from insects to mammals and able to bind PGN (non-catalytic PGRPs) and, in some cases, to efficiently degrade it (catalytic PGRPs). In Drosophila, several non-catalytic PGRPs function as selective peptidoglycan receptors upstream of the Toll and Imd pathways, the two major signalling cascades regulating the systemic production of antimicrobial peptides. Recognition PGRPs specifically activate the Toll pathway in response to Lys-type peptidoglycan found in most Gram-positive bacteria and the Imd pathway in response to DAP-type peptidoglycan encountered in Gram-positive bacilli-type bacteria and in Gram-negative bacteria. Catalytic PGRPs on the other hand can potentially reduce the level of immune activation by scavenging peptidoglycan. In accordance with this, PGRP-LB and PGRP-SC1A/B/2 have been shown to act as negative regulators of the Imd pathway. In this study, we report a biochemical and genetic analysis of PGRP-SB1, a catalytic PGRP. Our data show that PGRP-SB1 is abundantly secreted into the hemolymph following Imd pathway activation in the fat body, and exhibits an enzymatic activity towards DAP-type polymeric peptidoglycan. We have generated a PGRP-SB1/2 null mutant by homologous recombination, but its thorough phenotypic analysis did not reveal any immune function, suggesting a subtle role or redundancy of PGRP-SB1/2 with other molecules. Possible immune functions of PGRP-SB1 are discussed.Anna Zaidman-RémyMickael PoidevinMireille HervéDavid P WelchmanJuan C ParedesCarina FahlanderHakan SteinerDominique Mengin-LecreulxBruno LemaitrePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 2, p e17231 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anna Zaidman-Rémy Mickael Poidevin Mireille Hervé David P Welchman Juan C Paredes Carina Fahlander Hakan Steiner Dominique Mengin-Lecreulx Bruno Lemaitre Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.
description	Peptidoglycan is an essential and specific component of the bacterial cell wall and therefore is an ideal recognition signature for the immune system. Peptidoglycan recognition proteins (PGRPs) are conserved from insects to mammals and able to bind PGN (non-catalytic PGRPs) and, in some cases, to efficiently degrade it (catalytic PGRPs). In Drosophila, several non-catalytic PGRPs function as selective peptidoglycan receptors upstream of the Toll and Imd pathways, the two major signalling cascades regulating the systemic production of antimicrobial peptides. Recognition PGRPs specifically activate the Toll pathway in response to Lys-type peptidoglycan found in most Gram-positive bacteria and the Imd pathway in response to DAP-type peptidoglycan encountered in Gram-positive bacilli-type bacteria and in Gram-negative bacteria. Catalytic PGRPs on the other hand can potentially reduce the level of immune activation by scavenging peptidoglycan. In accordance with this, PGRP-LB and PGRP-SC1A/B/2 have been shown to act as negative regulators of the Imd pathway. In this study, we report a biochemical and genetic analysis of PGRP-SB1, a catalytic PGRP. Our data show that PGRP-SB1 is abundantly secreted into the hemolymph following Imd pathway activation in the fat body, and exhibits an enzymatic activity towards DAP-type polymeric peptidoglycan. We have generated a PGRP-SB1/2 null mutant by homologous recombination, but its thorough phenotypic analysis did not reveal any immune function, suggesting a subtle role or redundancy of PGRP-SB1/2 with other molecules. Possible immune functions of PGRP-SB1 are discussed.
format	article
author	Anna Zaidman-Rémy Mickael Poidevin Mireille Hervé David P Welchman Juan C Paredes Carina Fahlander Hakan Steiner Dominique Mengin-Lecreulx Bruno Lemaitre
author_facet	Anna Zaidman-Rémy Mickael Poidevin Mireille Hervé David P Welchman Juan C Paredes Carina Fahlander Hakan Steiner Dominique Mengin-Lecreulx Bruno Lemaitre
author_sort	Anna Zaidman-Rémy
title	Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.
title_short	Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.
title_full	Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.
title_fullStr	Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.
title_full_unstemmed	Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.
title_sort	drosophila immunity: analysis of pgrp-sb1 expression, enzymatic activity and function.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/34a45adc0e3245e6831bd0f56244a6f9
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Drosophila immunity: analysis of PGRP-SB1 expression, enzymatic activity and function.

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