ArticleThe Journal of biological chemistry2013
Characterization of Anopheles gambiae transglutaminase 3 (AgTG3) and its native substrate Plugin.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Article
- Current Status of Omics Studies Elucidating the Features of Reproductive Biology in Blood-Feeding Insects.Insects · 2023Review
- Silencing Transglutaminase GenesInsects · 2022Article
- Transglutaminase 3 negatively regulates immune responses on the heart of the mosquito, Anopheles gambiae.Scientific reports · 2022Article
- Physiological and Environmental Factors Affecting the Composition of the Ejaculate in Mosquitoes and Other Insects.Insects · 2019Review
- A transgenic tool to assess Anopheles mating competitiveness in the field.Parasites & vectors · 2018Article
- Article
- Heterosis Increases Fertility, Fecundity, and Survival of Laboratory-Produced F1 Hybrid Males of the Malaria Mosquito Anopheles coluzzii.G3 (Bethesda, Md.) · 2015Article
- A comparative analysis of reproductive biology of insect vectors of human disease.Current opinion in insect science · 2015Article
- Dihydroisoxazole inhibitors of Anopheles gambiae seminal transglutaminase AgTG3.Malaria journal · 2014Article
- Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Male Anopheles mosquitoes coagulate their seminal fluids via cross-linking of a substrate, called Plugin, by the seminal transglutaminase AgTG3. Formation of the "mating plug" by cross-linking Plugin is necessary for efficient sperm storage by females. AgTG3 has a similar degree of sequence identity (~30%) to both human Factor XIII (FXIII) and tissue transglutaminase 2 (hTG2). Here we report the solution structure and in vitro activity for the cross-linking reaction of AgTG3 and Plugin. AgTG3 is a dimer in solution and exhibits Ca(2+)-dependent nonproteolytic activation analogous to cytoplasmic FXIII. The C-terminal domain of Plugin is predominantly α-helical with extended tertiary structure and oligomerizes in solution. The specific activity of AgTG3 was measured as 4.25 × 10(-2) units mg(-1). AgTG3 is less active than hTG2 assayed using the general substrate TVQQEL but has 8-10× higher relative activity when Plugin is the substrate. Mass spectrometric analysis of cross-linked Plugin detects specific peptides including a predicted consensus motif for cross-linking by AgTG3. These results support the development of AgTG3 inhibitors as specific and effective chemosterilants for A. gambiae.
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Registered trials
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