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Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major.

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Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major. / McKean, Paul G.; Delahay, Rob; Pimenta, Paulo F. et al.
In: Molecular and Biochemical Parasitology, Vol. 85, No. 2, 04.1997, p. 221-231.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

McKean, PG, Delahay, R, Pimenta, PF & Smith, DF 1997, 'Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major.', Molecular and Biochemical Parasitology, vol. 85, no. 2, pp. 221-231. https://doi.org/10.1016/S0166-6851(97)02829-6

APA

Vancouver

McKean PG, Delahay R, Pimenta PF, Smith DF. Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major. Molecular and Biochemical Parasitology. 1997 Apr;85(2):221-231. doi: 10.1016/S0166-6851(97)02829-6

Author

McKean, Paul G. ; Delahay, Rob ; Pimenta, Paulo F. et al. / Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major. In: Molecular and Biochemical Parasitology. 1997 ; Vol. 85, No. 2. pp. 221-231.

Bibtex

@article{bcaa6447dc764a58b10f8c6e40feac3e,
title = "Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major.",
abstract = "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.",
keywords = "Leishmania major, Gene family, Surface proteins, Amino acid repeats",
author = "McKean, {Paul G.} and Rob Delahay and Pimenta, {Paulo F.} and Smith, {Deborah F.}",
year = "1997",
month = apr,
doi = "10.1016/S0166-6851(97)02829-6",
language = "English",
volume = "85",
pages = "221--231",
journal = "Molecular and Biochemical Parasitology",
issn = "0166-6851",
publisher = "Elsevier",
number = "2",

}

RIS

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 -