
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.
Microbial Viability, Science, Q, Fat Body, R, Pupa, Bombyx, Phosphoproteins, Anti-Bacterial Agents, Protein Subunits, Vitellogenins, Larva, Escherichia coli, Medicine, Animals, Research Article, Bacillus subtilis, Protein Binding
Microbial Viability, Science, Q, Fat Body, R, Pupa, Bombyx, Phosphoproteins, Anti-Bacterial Agents, Protein Subunits, Vitellogenins, Larva, Escherichia coli, Medicine, Animals, Research Article, Bacillus subtilis, Protein Binding
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