Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major.
AU - McKean, Paul G.
AU - Delahay, Rob
AU - Pimenta, Paulo F.
AU - Smith, Deborah F.
PY - 1997/4
Y1 - 1997/4
N2 - The LmcDNA16 gene family of Leishmania major contains five genes: three highly related sequences, genes A, B and C, and a tandem pair of unrelated 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 call. This paper describes the identification and characterisation of a second protein encoded by this gene array: the 7.6 kDa A/C protein. This molecule shares considerable amino acid identity with the gene B protein (GBP) but lacks the characteristic proline rich amino acid repeat region. Like GBP, the A/C protein is expressed on the surface of infective metacyclic parasites, despite the lack of conventional signal and anchor sequences. It has previously been suggested that the GBP repetitive sequence plays a role in mediating protein attachment to 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.
AB - The LmcDNA16 gene family of Leishmania major contains five genes: three highly related sequences, genes A, B and C, and a tandem pair of unrelated 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 call. This paper describes the identification and characterisation of a second protein encoded by this gene array: the 7.6 kDa A/C protein. This molecule shares considerable amino acid identity with the gene B protein (GBP) but lacks the characteristic proline rich amino acid repeat region. Like GBP, the A/C protein is expressed on the surface of infective metacyclic parasites, despite the lack of conventional signal and anchor sequences. It has previously been suggested that the GBP repetitive sequence plays a role in mediating protein attachment to 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.
KW - Leishmania major
KW - Gene family
KW - Surface proteins
KW - Amino acid repeats
U2 - 10.1016/S0166-6851(97)02829-6
DO - 10.1016/S0166-6851(97)02829-6
M3 - Journal article
VL - 85
SP - 221
EP - 231
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
SN - 0166-6851
IS - 2
ER -