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Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4.

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Harvard

Gram, GJ, Hemming, A, Bolmstedt, A, Jansson, B, Olofsson, S, Akerblom, L, Nielsen, JO & Hansen, JE 1994, 'Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4.' Archives of Virology, bind 139, nr. 3-4, s. 253-261.

APA

Gram, G. J., Hemming, A., Bolmstedt, A., Jansson, B., Olofsson, S., Akerblom, L., ... Hansen, J. E. (1994). Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4. Archives of Virology, 139(3-4), 253-261.

CBE

MLA

Vancouver

Author

Gram, G J ; Hemming, A ; Bolmstedt, A ; Jansson, B ; Olofsson, S ; Akerblom, L ; Nielsen, Jens Ole ; Hansen, J E. / Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4. I: Archives of Virology. 1994 ; Bind 139, Nr. 3-4. s. 253-261.

Bibtex

@article{2e383efd0b5942a38c1b8e531d0d1e30,
title = "Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4.",
abstract = "Glycosylation is necessary for HIV-1 gp120 to attain a functional conformation, and individual N-linked glycans of gp120 are important, but not essential, for replication of HIV-1 in cell culture. We have constructed a mutant HIV-1 infectious clone lacking a signal for N-linked glycosylation in the V1-loop of HIV-1 gp120. Lack of an N-linked glycan was verified by a mobility enhancement of mutant gp120 in SDS-gel electrophoresis. The mutated virus showed no differences in either gp120 content per infectious unit or infectivity, indicating that the N-linked glycan was neither essential nor affecting viral infectivity in cell culture. We found that the mutated virus lacking an N-linked glycan in the V1-loop of gp120 was more resistant to neutralization by monoclonal antibodies to the V3-loop and neutralization by soluble recombinant CD4 (sCD4). Both viruses were equally well neutralized by ConA and a conformation dependent human antibody IAM-2G12. This suggests that the N-linked glycan in the V1-loop modulates the three-dimensional conformation of gp120, without changing the overall functional integrity of the molecule.",
author = "Gram, {G J} and A Hemming and A Bolmstedt and B Jansson and S Olofsson and L Akerblom and Nielsen, {Jens Ole} and Hansen, {J E}",
year = "1994",
language = "English",
volume = "139",
pages = "253--261",
journal = "Archives of Virology",
issn = "0304-8608",
publisher = "Springer Wien",
number = "3-4",

}

RIS

TY - JOUR

T1 - Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4.

AU - Gram, G J

AU - Hemming, A

AU - Bolmstedt, A

AU - Jansson, B

AU - Olofsson, S

AU - Akerblom, L

AU - Nielsen, Jens Ole

AU - Hansen, J E

PY - 1994

Y1 - 1994

N2 - Glycosylation is necessary for HIV-1 gp120 to attain a functional conformation, and individual N-linked glycans of gp120 are important, but not essential, for replication of HIV-1 in cell culture. We have constructed a mutant HIV-1 infectious clone lacking a signal for N-linked glycosylation in the V1-loop of HIV-1 gp120. Lack of an N-linked glycan was verified by a mobility enhancement of mutant gp120 in SDS-gel electrophoresis. The mutated virus showed no differences in either gp120 content per infectious unit or infectivity, indicating that the N-linked glycan was neither essential nor affecting viral infectivity in cell culture. We found that the mutated virus lacking an N-linked glycan in the V1-loop of gp120 was more resistant to neutralization by monoclonal antibodies to the V3-loop and neutralization by soluble recombinant CD4 (sCD4). Both viruses were equally well neutralized by ConA and a conformation dependent human antibody IAM-2G12. This suggests that the N-linked glycan in the V1-loop modulates the three-dimensional conformation of gp120, without changing the overall functional integrity of the molecule.

AB - Glycosylation is necessary for HIV-1 gp120 to attain a functional conformation, and individual N-linked glycans of gp120 are important, but not essential, for replication of HIV-1 in cell culture. We have constructed a mutant HIV-1 infectious clone lacking a signal for N-linked glycosylation in the V1-loop of HIV-1 gp120. Lack of an N-linked glycan was verified by a mobility enhancement of mutant gp120 in SDS-gel electrophoresis. The mutated virus showed no differences in either gp120 content per infectious unit or infectivity, indicating that the N-linked glycan was neither essential nor affecting viral infectivity in cell culture. We found that the mutated virus lacking an N-linked glycan in the V1-loop of gp120 was more resistant to neutralization by monoclonal antibodies to the V3-loop and neutralization by soluble recombinant CD4 (sCD4). Both viruses were equally well neutralized by ConA and a conformation dependent human antibody IAM-2G12. This suggests that the N-linked glycan in the V1-loop modulates the three-dimensional conformation of gp120, without changing the overall functional integrity of the molecule.

M3 - Journal article

VL - 139

SP - 253

EP - 261

JO - Archives of Virology

JF - Archives of Virology

SN - 0304-8608

IS - 3-4

ER -

ID: 32506122