A genome-wide analysis in Anopheles gambiae mosquitoes reveals 46 male accessory gland genes, possible modulators of female behavior.
The male accessory glands (MAGs) of many insect species produce and secrete a number of reproductive proteins collectively named Acps. These proteins, many of which are rapidly evolving, are essential for male fertility and represent formidable modulators of female postmating behavior. Upon copulation, the transfer of Acps has been shown in Drosophila and other insects to trigger profound physiological and behavioral changes in females, including enhanced ovulation/oviposition and reduced mating receptivity. In Anopheles gambiae mosquitoes, the principal vectors of human malaria, experimental evidence clearly demonstrates a key role of MAG products in inducing female responses. However, no Acp has been experimentally identified to date in this or in any other mosquito species. In this study we report on the identification of 46 MAG genes from An. gambiae, 25 of which are male reproductive tract-specific. This was achieved through a combination of bioinformatics searches and manual annotation confirmed by transcriptional profiling. Among these genes are the homologues of 40% of the Drosophila Acps analyzed, including Acp70A, or sex peptide, which in the fruit fly is the principal modulator of female postmating behavior. Although many Anopheles Acps belong to the same functional classes reported for Drosophila, suggesting a conserved role for these proteins in mosquitoes, some represent novel lineage-specific Acps that may have evolved to perform functions relevant to Anopheles reproductive behavior. Our findings imply that the molecular basis of Anopheles female postmating responses can now be studied, opening novel avenues for the field control of these important vectors of human disease.
Dottorini
Tania
T
Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università degli Studi di Perugia, Via Del Giochetto, 06122 Perugia, Italy.
Nicolaides
Lietta
L
Ranson
Hilary
H
Rogers
David W
DW
Crisanti
Andrea
A
Catteruccia
Flaminia
F
D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000235:genetics* / Q000472:pathogenicity / Q000502:physiology*; D004330:Drosophila / Q000235:genetics; D029721:Drosophila Proteins / Q000235:genetics; D019143:Evolution, Molecular; D005260:Female; D015870:Gene Expression; D017344:Genes, Insect; D005837:Genitalia, Male / Q000502:physiology; D049750:Genome, Insect; D012739:Gonadal Steroid Hormones / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D006801:Humans; D007301:Insect Hormones / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics; D010802:Phylogeny; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D012726:Sexual Behavior, Animal / Q000502:physiology*; D013045:Species Specificity; D036341:Intercellular Signaling Peptides and Proteins
D029721:Drosophila Proteins; D012739:Gonadal Steroid Hormones; D007301:Insect Hormones; D010455:Peptides; D015842:Serine Proteinase Inhibitors; C056736:SP protein, Drosophila; D036341:Intercellular Signaling Peptides and Proteins