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Cloning and characterization of a cDNA encoding a male‐specific serum protein of the Mediterranean fruit fly, Ceratitis capitata , with sequence similarity to odourant–binding proteins
Author(s) -
Thymlanou S.,
Mavroidis M.,
Kokolakis G.,
Komitopoulou K.,
Zacharopoulou A.,
Mintzas A. C.
Publication year - 1998
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.1998.740345.x
Subject(s) - ceratitis capitata , biology , complementary dna , gene , peptide sequence , cloning (programming) , genetics , signal peptide , amino acid , protein sequencing , nucleic acid sequence , coding region , genome , microbiology and biotechnology , botany , tephritidae , pest analysis , computer science , programming language
Male‐specific serum proteins (MSSPs) are low molecular weight proteins which accumulate in high amounts in the haemolymph of adult males of the medfly Ceratitis capitata . By screening an expression library with anti‐MSSP antibodies, we have isolated and determined the nucleotide sequence of a cDNA clone coding for one of the male‐specific polypeptides (MSSP‐α). The MSSP‐α mRNA encodes a polypeptide of 144 amino acids with a secretory signal sequence of sixteen amino acids. Southern analysis indicated that there are multiple copies of MSSP genes in the medfly genome. Northern analysis showed that the MSSP mRNAs are synthesized only in adult males. The accumulation pattern of these mRNAs during development suggests that the expression of the MSSP genes is developmentally regulated at both transcriptional and translational levels. The predicted peptide sequence of MSSP‐α shows significant similarity to a group of pheromone‐ and general odourant‐binding proteins of insects.