LP30K protein manifested in hemocytes of Bombyx mori larva on Nosema bombycis infection and showed functional evolution based on glucose- binding domain.

ABSTRACT: Infection by microsporidian Nosema bombycis induced appearance of exclusive protein conjugate of 190 kDa in hemocytes of silkworm Bombyx mori L (Lepidoptera: Bombycidae). Mass spectrometry of the band showed peptides of low molecular weight 30 kDa lipoprotein (LP30K). Six accessions of LP30K identified from the hemocytes comprised 30 K lipoprotein 1, 30 K protein 1, 2, 6, 7 and 11. Two uncharacterised proteins (UCP) identified from the hemocytes showed 100% similarity with LP30K sequence, altogether showed abundance after the infection. The LP30K accessions H9J4F6 (Q00802), E5EVW2 and the UCP accessions D4QGC0 and D4QGB9 showed presence of glucose binding protein I domain "ADSDVPNDILEEQLYNSIVVADYDSAVEK" that binds with fungal glucans to inhibit infection. However glucose bind

SUBMITTER: Shambhavi HP 

PROVIDER: S-EPMC10317940 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature