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Characterization of body louse midgut proteins recognized by resistant hosts



Characterization of body louse midgut proteins recognized by resistant hosts



Medical and Veterinary Entomology 10(1): 35-38



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-1, F-2, F-3, and F-4) when resolved on a 18% SDS-PAGE. The F-1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.

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Accession: 002775522

Download citation: RISBibTeXText

PMID: 8834740

DOI: 10.1111/j.1365-2915.1996.tb00079.x


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