A modular chitin-binding protease associated with hemocytes and hemolymph in the mosquito Anopheles gambiae.
Sp22D, a modular serine protease encompassing chitin binding, low density lipoprotein receptor, and scavenger receptor cysteine-rich domains, was identified by molecular cloning in the malaria vector, Anopheles gambiae. It is expressed in multiple body parts and during much of development, most intensely in hemocytes. The protein appears to be posttranslationally modified. Its integral, putatively glycosylated form is secreted in the hemolymph, whereas a smaller form potentially generated by proteolytic processing is associated with the tissues. Bacterial challenge or wounding result in low-level RNA induction, but the protein does not bind to bacteria, nor is its processing affected by infection. However, Sp22D binds to chitin with high affinity and undergoes transient changes in processing during pupal to adult metamorphosis; it may respond to exposure to naked chitin during tissue remodeling or damage.
Danielli
A
A
European Molecular Biology Laboratory, Meyerhofstrasse, 1, 69117 Heidelberg, Germany.
Loukeris
T G
TG
Lagueux
M
M
Müller
H M
HM
Richman
A
A
Kafatos
F C
FC
D000818:Animals; D000852:Anopheles / Q000201:enzymology*; D002686:Chitin / Q000378:metabolism*; D006434:Hemocytes / Q000201:enzymology*; D006458:Hemolymph / Q000201:enzymology*; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000378:metabolism*
D002686:Chitin; D012697:Serine Endopeptidases