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SM1 is a twelve-amino-acid peptide that binds tightly to the  Anopheles  salivary gland and inhibits its invasion by  Plasmodium  sporozoites. By use of UV-crosslinking experiments between the peptide and its salivary gland target protein, we have identified the  Anopheles  salivary protein, saglin, as the receptor for SM1. Furthermore, by use of an anti-SM1 antibody, we have determined that the peptide is a mimotope of the  Plasmodium  sporozoite Thrombospondin Related Anonymous Protein (TRAP). TRAP binds to saglin with high specificity. Point mutations in TRAP's binding domain A abrogate binding, and binding is competed for by the SM1 peptide. Importantly,  in vivo  down-regulation of saglin expression results in strong inhibition of salivary gland invasion. Together, the results suggest that saglin/TRAP interaction is crucial for salivary gland invasion by  Plasmodium  sporozoites.

Malaria Parasite Invasion of the Mosquito Salivary Gland Requires Interaction between the Plasmodium TRAP and the Anopheles Saglin Proteins