Search bioRxiv⌕ Search

Biology subjects

Sivabalakrishnan, K.

Publications and source records attributed to Sivabalakrishnan, K..

2 recordsLinked to original sources

Preimaginal development of Aedes aegypti in brackish water produces adult mosquitoes with thicker cuticles and greater insecticide resistance

Aedes aegypti and Aedes albopictus mosquitoes, the principal vectors of many human arboviral diseases, lay eggs and undergo preimaginal development in fresh water habitats. They have also recently been found to develop in brackish water in coastal areas. Adult females emerging from brackish water-developing Ae. aegypti larvae are shown to possess thicker cuticles and greater resistance to common insecticides used against adults (adulticides) compared with fresh water Ae. aegypti. These findings are compatible with previous findings showing that brackish water Ae. aegypti larvae possess thicker cuticles and greater larvicide resistance. Greater resistance of salinity-tolerant Ae. aegypti to adulticides and larvicides is a hitherto unappreciated problem for controlling arboviral diseases and has implications also for other mosquito-borne diseases.

zoology↗

Lectin Microarray Analysis of Salivary Gland Glycoproteins from the Arboviral Vector Aedes aegypti and the Malaria Vector Anopheles stephensi

Salivary gland glycoconjugates in human-feeding insects and arachnids can elicit hypersensitivity reactions. Glycoproteins introduced during blood feeding by arachnid ticks are responsible for red meat allergy or the -gal syndrome. Dengue virus transmitted by Aedes mosquitoes incorporates mosquito glycoproteins into its envelope and malaria parasites transmitted by Anopheles mosquitoes reportedly express -gal epitopes that are potentially derived from mosquito salivary glands. Tick salivary gland glycoproteins possess -gal epitopes. We used microarrays containing forty different lectins to analyse salivary gland protein glycoconjugates from the principal arboviral vector Aedes aegypti and the rapidly spreading malaria vector Anopheles stephensi. Salivary gland glycoproteins of both mosquitoes possessed very similar lectin-binding specificities. Lectin-binding profiles showed the significant presence of oligomannose N-glycans and O-glycans, a limited presence of glycan structures capped with terminal GalNAc, GlcNAc, {beta} linked Gal, 1-6 linked fucose, and no detectable sialic acids or terminal -linked Gal in salivary gland glycoproteins.

zoology↗