A genome-wide analysis in Anopheles gambiae mosquitoes reveals 46 male accessory gland genes, possible modulators of female behavior

被引:106
作者
Dottorini, Tania
Nicolaides, Liettal
Ranson, Hilary
Rogers, David W.
Crisanti, Andrea
Catteruccia, Flaminia
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, London SW7 2AZ, England
[2] Univ Perugia, Dipartimento Med Sperimentale & Sci Biochim, I-06122 Perugia, Italy
基金
英国惠康基金; 英国医学研究理事会;
关键词
reproduction; malaria; mating; Acp; seminal fluid;
D O I
10.1073/pnas.0703904104
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:16215 / 16220
页数:6
相关论文
共 38 条
[1]   Molecular evolution of seminal proteins in field crickets [J].
Andres, Jose A. ;
Maroja, Luana S. ;
Bogdanowicz, Steven M. ;
Swanson, Willie J. ;
Harrison, Richard G. .
MOLECULAR BIOLOGY AND EVOLUTION, 2006, 23 (08) :1574-1584
[2]   Localization and significance of molecular chaperones, heat shock protein 1, and tumor rejection antigen gp96 in the male reproductive tract and during capacitation and acrosome reaction [J].
Asquith, KL ;
Harman, AJ ;
McLaughlin, EA ;
Nixon, B ;
Aitken, RJ .
BIOLOGY OF REPRODUCTION, 2005, 72 (02) :328-337
[3]   Large clusters of co-expressed genes in the Drosophila genome [J].
Boutanaev, AM ;
Kalmykova, AI ;
Shevelyov, YY ;
Nurminsky, DI .
NATURE, 2002, 420 (6916) :666-669
[5]   FURTHER STUDIES ON CONSECUTIVE MATINGS IN ANOPHELES-GAMBIAE COMPLEX [J].
BRYAN, JH .
NATURE, 1972, 239 (5374) :519-+
[6]   An Anopheles transgenic sexing strain for vector control [J].
Catteruccia, F ;
Benton, JP ;
Crisanti, A .
NATURE BIOTECHNOLOGY, 2005, 23 (11) :1414-1417
[7]   Functions and analysis of the seminal fluid proteins of male Drosophila melanogaster fruit flies [J].
Chapman, T ;
Davies, SJ .
PEPTIDES, 2004, 25 (09) :1477-1490
[8]   Cloning of the gene encoding the antibacterial peptide drosocin involved in Drosophila immunity - Expression studies during the immune response [J].
Charlet, M ;
Lagueux, M ;
Reichhart, JM ;
Hoffmann, D ;
Braun, A ;
Meister, M .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 241 (03) :699-706
[9]   A MALE ACCESSORY-GLAND PEPTIDE THAT REGULATES REPRODUCTIVE-BEHAVIOR OF FEMALE DROSOPHILA-MELANOGASTER [J].
CHEN, PS ;
STUMMZOLLINGER, E ;
AIGAKI, T ;
BALMER, J ;
BIENZ, M ;
BOHLEN, P .
CELL, 1988, 54 (03) :291-298
[10]  
CLARK AG, 1995, GENETICS, V139, P189