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Characterization of body louse midgut proteins recognized by resistant hosts
Author(s) -
OCHANDA JAMES O.,
MUMCUOGLU KOSTA Y.,
BENYAKIR DAVID,
OKURU J. K.,
ODUOL V. O.,
GALUN RACHEL
Publication year - 1996
Publication title -
medical and veterinary entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 82
eISSN - 1365-2915
pISSN - 0269-283X
DOI - 10.1111/j.1365-2915.1996.tb00079.x
Subject(s) - polyclonal antibodies , biology , midgut , microbiology and biotechnology , western blot , electroelution , gel electrophoresis , antibody , trypsinization , molecular mass , polyacrylamide gel electrophoresis , biochemistry , trypsin , gene , enzyme , immunology , botany , larva
. The human body louse, Pediculus humanus , showed eighteen midgut proteins ranging between 12 and 117 kDa, when analysed by SDS‐PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F, F 2 , F 3 , and F 4 ) when resolved on a 18% SDS‐PAGE. The Fj fragment of the 35 kDa protein reacted with me polyclonal antibodies by the immunoblot technique.