Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.

Silkworm, Bombyx mori, vitellogenin (Vg) was isolated from perivisceral fat body of day 3 of pupa. Both Vg subunits were co-purified as verified by mass spectrometry and immunoblot. Purified Vg responded to specific tests for major posttranslational modifications on native gels indicating its nature...

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Main Authors: Nitin Kumar Singh, Britto Cathrin Pakkianathan, Manish Kumar, Tulika Prasad, Mani Kannan, Simone König, Muthukalingan Krishnan
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3772815?pdf=render
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spelling doaj-e84c553a25f14042b0d7c121d0cae9852020-11-24T21:54:19ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0189e7300510.1371/journal.pone.0073005Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.Nitin Kumar SinghBritto Cathrin PakkianathanManish KumarTulika PrasadMani KannanSimone KönigMuthukalingan KrishnanSilkworm, Bombyx mori, vitellogenin (Vg) was isolated from perivisceral fat body of day 3 of pupa. Both Vg subunits were co-purified as verified by mass spectrometry and immunoblot. Purified Vg responded to specific tests for major posttranslational modifications on native gels indicating its nature as lipo-glyco-phosphoprotein. The Vg fraction had strong antibacterial activity against Gram negative bacterium Escherichia coli and Gram positive bacterium Bacillus subtilis. Microscopic images showed binding of Vg to bacterial cells and their destruction. When infected silkworm larvae were treated with purified Vg they survived the full life cycle in contrast to untreated animals. This result showed that Vg has the ability to inhibit the proliferation of bacteria in the silkworm fluid system without disturbing the regular metabolism of the host.http://europepmc.org/articles/PMC3772815?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Nitin Kumar Singh
Britto Cathrin Pakkianathan
Manish Kumar
Tulika Prasad
Mani Kannan
Simone König
Muthukalingan Krishnan
spellingShingle Nitin Kumar Singh
Britto Cathrin Pakkianathan
Manish Kumar
Tulika Prasad
Mani Kannan
Simone König
Muthukalingan Krishnan
Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.
PLoS ONE
author_facet Nitin Kumar Singh
Britto Cathrin Pakkianathan
Manish Kumar
Tulika Prasad
Mani Kannan
Simone König
Muthukalingan Krishnan
author_sort Nitin Kumar Singh
title Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.
title_short Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.
title_full Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.
title_fullStr Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.
title_full_unstemmed Vitellogenin from the silkworm, Bombyx mori: an effective anti-bacterial agent.
title_sort vitellogenin from the silkworm, bombyx mori: an effective anti-bacterial agent.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2013-01-01
description Silkworm, Bombyx mori, vitellogenin (Vg) was isolated from perivisceral fat body of day 3 of pupa. Both Vg subunits were co-purified as verified by mass spectrometry and immunoblot. Purified Vg responded to specific tests for major posttranslational modifications on native gels indicating its nature as lipo-glyco-phosphoprotein. The Vg fraction had strong antibacterial activity against Gram negative bacterium Escherichia coli and Gram positive bacterium Bacillus subtilis. Microscopic images showed binding of Vg to bacterial cells and their destruction. When infected silkworm larvae were treated with purified Vg they survived the full life cycle in contrast to untreated animals. This result showed that Vg has the ability to inhibit the proliferation of bacteria in the silkworm fluid system without disturbing the regular metabolism of the host.
url http://europepmc.org/articles/PMC3772815?pdf=render
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