Pg. Mckean et al., CHARACTERIZATION OF A 2ND PROTEIN ENCODED BY THE DIFFERENTIALLY REGULATED LMCDNA16-GENE FAMILY OF LEISHMANIA-MAJOR, Molecular and biochemical parasitology, 85(2), 1997, pp. 221-231
The LmcDNA16 gene family of Leishmania major contains five genes: thre
e highly related sequences, genes A, B and C, and a tandem pair of unr
elated sequences, genes D1 and D2. Previous studies have demonstrated
that gene B codes for a novel, hydrophilic protein that is present on
the surface of infective parasite stages at approximately 10(5) copies
per cell. This paper describes the identification and characterisatio
n of a second protein encoded by this gene array: the 7.6 kDa A/C prot
ein. This molecule shares considerable amino acid identity with the ge
ne B protein (GBP) but lacks the characteristic proline rich amino aci
d repeat region. Like GBP, the A/C protein is expressed on the surface
of infective metacyclic parasites, despite the lack of conventional s
ignal and anchor sequences. It has previously been suggested that the
GBP repetitive sequence plays a role in mediating protein attachment t
o the parasite surface. It now appears more likely that the conserved
amino- and/or carboxyl-terminal domains of the A/C and B proteins are
involved in this process. (C) 1997 Elsevier Science B.V.