Peptidoglycan Recognition Protein S2 from Silkworm Integument: Characterization, Microbe-Induced Expression, and Involvement in the Immune-Deficiency Pathway

Peptidoglycan recognition protein (PGRP) binds specifically to peptidoglycan and plays an important role as a pattern recognition receptor in the innate immunity of insects. The cDNA of a short-type PGRP, an open reading frame of 588 bp encoding a polypeptide of 196 amino acids, was cloned from Bomb...

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Veröffentlicht in:Journal of insect science (Tucson, Ariz.) Ariz.), 2015, Vol.15 (20), p.1-6
Hauptverfasser: Yang, Jie, Wang, Xiaonan, Tang, Shunming, Shen, Zhongyuan, Wu, Jinmei
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Wang, Xiaonan
Tang, Shunming
Shen, Zhongyuan
Wu, Jinmei
description Peptidoglycan recognition protein (PGRP) binds specifically to peptidoglycan and plays an important role as a pattern recognition receptor in the innate immunity of insects. The cDNA of a short-type PGRP, an open reading frame of 588 bp encoding a polypeptide of 196 amino acids, was cloned from Bombyx mori. A phylogenetic tree was constructed, and the results showed that BmPGRP-S2 was most similar to Drosophila melanogaster PGRP (DmPGRP-SA). The induced expression profile of BmPGRP-S2 in healthy Escherichia coli- and Bacillus subtilis-challenged B. mori was measured using semiquantitative reverse transcriptase polymerase chain reaction analysis. The expression of BmPGRP-S2 was upregulated at 24 h by E. coli and Ba. subtilis challenge. In addition, in the integument of B. mori, RNAi knockdown of BmPGRP-S2 caused an obvious reduction in the transcription expression of the transcription factor Relish and in antibacterial effector genes Attacin, Gloverin, and Moricin. The results indicated that BmPGRP-S2 participates in the signal transduction pathway of B. mori.
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The cDNA of a short-type PGRP, an open reading frame of 588 bp encoding a polypeptide of 196 amino acids, was cloned from Bombyx mori. A phylogenetic tree was constructed, and the results showed that BmPGRP-S2 was most similar to Drosophila melanogaster PGRP (DmPGRP-SA). The induced expression profile of BmPGRP-S2 in healthy Escherichia coli- and Bacillus subtilis-challenged B. mori was measured using semiquantitative reverse transcriptase polymerase chain reaction analysis. The expression of BmPGRP-S2 was upregulated at 24 h by E. coli and Ba. subtilis challenge. In addition, in the integument of B. mori, RNAi knockdown of BmPGRP-S2 caused an obvious reduction in the transcription expression of the transcription factor Relish and in antibacterial effector genes Attacin, Gloverin, and Moricin. The results indicated that BmPGRP-S2 participates in the signal transduction pathway of B. mori.</description><identifier>ISSN: 1536-2442</identifier><identifier>EISSN: 1536-2442</identifier><language>eng</language><publisher>University of Wisconsin Library</publisher><subject>amino acids ; barium ; Bombyx mori ; complementary DNA ; Drosophila melanogaster ; Escherichia coli ; genes ; innate immunity ; integument ; open reading frames ; peptidoglycans ; phylogeny ; polypeptides ; reverse transcriptase polymerase chain reaction ; RNA interference ; signal transduction ; silkworms ; transcription factors</subject><ispartof>Journal of insect science (Tucson, Ariz.), 2015, Vol.15 (20), p.1-6</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,4012</link.rule.ids></links><search><creatorcontrib>Yang, Jie</creatorcontrib><creatorcontrib>Wang, Xiaonan</creatorcontrib><creatorcontrib>Tang, Shunming</creatorcontrib><creatorcontrib>Shen, Zhongyuan</creatorcontrib><creatorcontrib>Wu, Jinmei</creatorcontrib><title>Peptidoglycan Recognition Protein S2 from Silkworm Integument: Characterization, Microbe-Induced Expression, and Involvement in the Immune-Deficiency Pathway</title><title>Journal of insect science (Tucson, Ariz.)</title><description>Peptidoglycan recognition protein (PGRP) binds specifically to peptidoglycan and plays an important role as a pattern recognition receptor in the innate immunity of insects. The cDNA of a short-type PGRP, an open reading frame of 588 bp encoding a polypeptide of 196 amino acids, was cloned from Bombyx mori. A phylogenetic tree was constructed, and the results showed that BmPGRP-S2 was most similar to Drosophila melanogaster PGRP (DmPGRP-SA). The induced expression profile of BmPGRP-S2 in healthy Escherichia coli- and Bacillus subtilis-challenged B. mori was measured using semiquantitative reverse transcriptase polymerase chain reaction analysis. The expression of BmPGRP-S2 was upregulated at 24 h by E. coli and Ba. subtilis challenge. In addition, in the integument of B. mori, RNAi knockdown of BmPGRP-S2 caused an obvious reduction in the transcription expression of the transcription factor Relish and in antibacterial effector genes Attacin, Gloverin, and Moricin. 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The cDNA of a short-type PGRP, an open reading frame of 588 bp encoding a polypeptide of 196 amino acids, was cloned from Bombyx mori. A phylogenetic tree was constructed, and the results showed that BmPGRP-S2 was most similar to Drosophila melanogaster PGRP (DmPGRP-SA). The induced expression profile of BmPGRP-S2 in healthy Escherichia coli- and Bacillus subtilis-challenged B. mori was measured using semiquantitative reverse transcriptase polymerase chain reaction analysis. The expression of BmPGRP-S2 was upregulated at 24 h by E. coli and Ba. subtilis challenge. In addition, in the integument of B. mori, RNAi knockdown of BmPGRP-S2 caused an obvious reduction in the transcription expression of the transcription factor Relish and in antibacterial effector genes Attacin, Gloverin, and Moricin. The results indicated that BmPGRP-S2 participates in the signal transduction pathway of B. mori.</abstract><pub>University of Wisconsin Library</pub><tpages>6</tpages></addata></record>
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subjects amino acids
barium
Bombyx mori
complementary DNA
Drosophila melanogaster
Escherichia coli
genes
innate immunity
integument
open reading frames
peptidoglycans
phylogeny
polypeptides
reverse transcriptase polymerase chain reaction
RNA interference
signal transduction
silkworms
transcription factors
title Peptidoglycan Recognition Protein S2 from Silkworm Integument: Characterization, Microbe-Induced Expression, and Involvement in the Immune-Deficiency Pathway
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