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 binding protein II domain "TLAPRTDDVLAEQLYMSVVIGEYETAIAK" is absent in LP30K accessions from hemocytes showed loss of DNA sequences encoding the domain. The accessions H9J4F5, H9B440, A7LIK7 and H9B444 showed 92% identity with B. mori LP30K protein (NP_001095198.2) however the glucose binding domain I is absent in these accessions suggesting isoform- specific restricted fungal defense activity. Phylogeny tree of the LP30K homologues showed four groups including microvitellogenin and 30 kDa proteins showing functional diversity endorsed with evolutionary diversity. LP30K accessions with glucose binding domain diverged from that without glucose binding domain exemplify co-evolution for domain- dependent functional roles like storage and immune reactions. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13205-023-03685-x.