Premium
Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae
Author(s) -
Kanost Michael R.,
Zepp Melissa K.,
Ladendorff Noma E.,
Andersson Laura A.
Publication year - 1994
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940270205
Subject(s) - manduca sexta , hemolymph , biology , sphingidae , manduca , galleria mellonella , biochemistry , lepidoptera genitalia , instar , bombyx mori , insect , larva , microbiology and biotechnology , botany , virulence , gene
A protein that inhibits hemocyte aggregation has been isolated from hemolymph of Manduca sexta larvae and named hemocyte aggregation inhibitor protein (HAIP). HAIP has a M r = 50,000, pI = 8.5, and contains 7% carbohydrate. It is present at 230 ± 20 μg/ml in hemolymph of day 3 fifth instar larvae. Antibodies to HAIP do not cross‐react with M. sexta hemolin, which is similar in size and charge and also inhibits hemocyte aggregation. HAIP and hemolin have some similarity in amino acid composition and NH 2 ‐terminal sequence, but are different in overall secondary structure, as determined by CD spectroscopy. The concentration of HAIP in hemolymph is not affected by injection of larvae with bacteria. A protein of approximately 50,000 daltons that reacts with antibody to M. sexta HAIP is present in hemolymph of Bombyx mori, Heliothis zea , and Galleria mellonella . Although the function of HAIP in vivo is not yet clear, it may have a role in modulating adhesion of hemocytes during defensive responses. © 1994 Wiley‐Liss, Inc.