| a novel c-type lectin in the black tiger shrimp penaeus monodon functions as a pattern recognition receptor by binding and causing bacterial agglutination. | c-type lectins are pattern recognition proteins that play important roles in innate immunity in invertebrates by mediating the recognition of pathogens. in this study, a novel c-type lectin gene, pmclec, was cloned and characterized from the black tiger shrimp penaeus monodon. the open reading frame of pmclec is 657 bp in length. it encodes a predicted protein of 218 amino acids with a calculated molecular mass and an isoelectric point of 24086 da and 4.67, respectively. sequence analysis of pmc ... | 2017 | 27876622 |
| domain inhibitory and bacteriostatic activities of the five-domain kazal-type serine proteinase inhibitor from black tiger shrimp penaeus monodon. | serine proteinase inhibitors (spis) in multi-cellular organisms are important modulators of proteinase activities in various biological processes. a five-domain kazal-type spi spipm2 from the black tiger shrimp penaeus monodon is presumably involved in innate immune response. the spipm2 with the domain p1 residues t, a, e, k and e was isolated from the hemocyte cdna libraries and found to strongly inhibit subtilisin and elastase, and weakly inhibit trypsin. to unravel further the inhibitory acti ... | 2009 | 18930077 |
| kazal-type serine proteinase inhibitors from the black tiger shrimp penaeus monodon and the inhibitory activities of spipm4 and 5. | serine proteinase inhibitors (spis) play important roles in physiological and immunological processes involving proteinases in all multicellular organisms. in black tiger shrimp penaeus monodon, nine different kazal-type spis, namely spipm1-9, were identified from the cdna libraries of hemocyte, hepatopancreas, hematopoietic tissue, ovary and lymphoid organ. they are multi-domain spis containing 2-7 and possibly more kazal domains. two interesting cdna clones, spipm4 and spipm5 coding for two-do ... | 2009 | 19497371 |