Journal
GENOMICS
Volume 93, Issue 4, Pages 367-375Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ygeno.2008.12.010
Keywords
Bombyx mori; Insect immunity; Serine protease inhibitor; Hemolymph protein; Melanization; Spatzle processing
Funding
- National Institutes of Health [GM58634]
- Oklahoma Agricultural Experimental Station [OKLO2450]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM058634] Funding Source: NIH RePORTER
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Serine protease inhibitors (serpins) are a superfamily of proteins, most of which control protease-mediated processes by inhibiting their cognate enzymes. Sequencing of the silkworm genome provides an opportunity to investigate serpin structure, function, and evolution at the genome level. There are thirty-four serpin genes in Bombyx mori. Six are highly similar to their Manduca sexta orthologs that regulate innate immunity. Three alternative exons in serpin1 gene and four in serpin28 encode a variable region including the reactive site loop. Splicing of serpin2 pre-mRNA yields variations in serpin2A, 2A' and 2B. Sequence similarity and intron positions reveal the evolutionary pathway of seven serpin genes in group C. RT-PCR indicates an increase in the mRNA levels of serpin1, 3, 5, 6, 9,12,13, 25, 27, 32 and 34 in fat body and hemocytes of larvae injected with bacteria. These results suggest that the silkworm serpins play regulatory roles in defense responses. (C) 2009 Elsevier Inc. All rights reserved.
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