Since ancient times, plant and microbial products were used in various aspects. However, their use against insects decreased when chemical products became developed.
Transposon-mediated transformation was used to produce Anopheles stephensi that express single-chain antibodies (scFvs) designed to target the human malaria parasite, Plasmodium falciparum.
Two alternative kdr-like mutations, L1014S and L1014F, were detected in An. stephensi with a high allelic frequency of L1014S.
Our studies on two putative blood-meal induced, midgut-specific promoters validate the use of G12 upstream regulatory regions to drive targeted transgene expression coinciding spatially and temporally with pre-sporogonic stages of Plasmodium parasites in the mosquito, offering the possibility of manipulating vector competence or performing functional studies on vector-parasite interactions.
Our findings support an emerging view with a possible role of proboscis as important equipment during host-seeking, and give us an insight into how these appendages likely evolved from a common origin in order to function as antenna organs.
The highly expressed D7 protein family of mosquito saliva has previously been shown to act as an anti-inflammatory mediator by binding host biogenic amines and cysteinyl leukotrienes (CysLTs).
The effect of the range of temperature on the thermal adaptation in Anopheles stephensi Liston 1901 was evaluated in the laboratory. Late third instar larvae of An. stephensi were exposed to variable temperatures viz. 37°C, 39°C, 41°C, 43°C and 45°C, and their lethal time to cause 50% mortality (LTM50) values were calculated.
A greater understanding of the development of the malaria parasite within the mosquito is required to fully evaluate the impact of TBIs.
Here we report the sequence analysis of the Rdl gene from Asian main malaria mosquito, Anopheles stephensi, using specific primers in the polymerase chain reaction.
Physical mapping is a useful approach for studying genome organization and evolution as well as for genome sequence assembly.