PCR Cloning of a Divalent Metal Transporter From Malaria Mosquito <i>Anopheles gambiae</i> tissue cDNA library

Metal ions are vital for many biological processes, such as transcription, respiration and growth (Schaffner et al . 2006)and essential cofactors for oxidative phosphorylation, gene regulation and free‐radical homeostasis. Failure to maintain appropriate levels of metal ions in humans could cause metal ion deficiency disorders, and neurodegenerative diseases (Hediger et al . 1997). The regulation of metal ion transport within neurons is critical for normal brain function (Howitt et al . 2009). Acquisition of metal transition (Zn, Cu, Fe) is mediated by a specific high affinity divalent metal transporter which belongs to a cation efflux protein family with predicted twelve trans‐membrane domains and found to increase tolerance to divalent metal ions like zinc. These proteins are considered to be efflux pumps that remove these ions from cells. Divalent metal transporter 1 (DMT1) is a widely expressed metal ion transporter that is vital for intestinal iron absorption and iron utilization by most cell types throughout the body (Hediger et al . 2007). Cloning and functional characterization of DMT1/NRAMP homolog is reported in mosquito Anopheles albimanus (Martinez‐Barnetche et al . 2008). In this present study, we report the cloning of a divalent metal transporter fragment (~500 bp) from Anopheles gambiae tissue cDNA library by polymerase chain reaction. Supported by Dept of ED HBCU INST AID P031B070074.