Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins.

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Standard

Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins. / Hansen, J E; Nielsen, C M; Nielsen, C; Heegaard, P; Mathiesen, Lars Reinhardt; Nielsen, Jens Ole.

I: AIDS, Bind 3, Nr. 10, 1989, s. 635-641.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning

Harvard

Hansen, JE, Nielsen, CM, Nielsen, C, Heegaard, P, Mathiesen, LR & Nielsen, JO 1989, 'Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins.', AIDS, bind 3, nr. 10, s. 635-641. <http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2574581&query_hl=44>

APA

Hansen, J. E., Nielsen, C. M., Nielsen, C., Heegaard, P., Mathiesen, L. R., & Nielsen, J. O. (1989). Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins. AIDS, 3(10), 635-641. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2574581&query_hl=44

Vancouver

Hansen JE, Nielsen CM, Nielsen C, Heegaard P, Mathiesen LR, Nielsen JO. Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins. AIDS. 1989;3(10):635-641.

Author

Hansen, J E ; Nielsen, C M ; Nielsen, C ; Heegaard, P ; Mathiesen, Lars Reinhardt ; Nielsen, Jens Ole. / Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins. I: AIDS. 1989 ; Bind 3, Nr. 10. s. 635-641.

Bibtex

@article{73ed14e8507a441185c1f35088f3c54c,
title = "Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins.",
abstract = "The binding of 13 different lectins to gp120 partially purified from two HIV-1 isolates and one HIV-2 isolate was studied by in situ staining on electrophoretically separated and electroblotted HIV antigens. The lectins concanavalin A, wheat germ agglutinin, Lens culinaris agglutinin, Vicia faba agglutinin, Pisum sativum agglutinin and phytohaem(erythro)agglutinin bound to gp120 of all three isolates. The carbohydrate of gp120 recognized by lectins was thus arranged in at least four types of glycans: a high mannose type glycan, a bisected hybrid or complex type glycan, a biantennary fucosylated complex type glycan and a triantennary bisected complex type glycan. Only lectins which bound at least one of the four types of glycans were capable of inhibiting fusion of HIV-infected cells with CD4 cells by a carbohydrate-specific interaction with the HIV-infected cells. Thus, several different glycan structures may be implicated in CD4-gp120 binding.",
author = "Hansen, {J E} and Nielsen, {C M} and C Nielsen and P Heegaard and Mathiesen, {Lars Reinhardt} and Nielsen, {Jens Ole}",
year = "1989",
language = "English",
volume = "3",
pages = "635--641",
journal = "AIDS",
issn = "1350-2840",
publisher = "Lippincott Williams & Wilkins, Ltd.",
number = "10",

}

RIS

TY - JOUR

T1 - Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins.

AU - Hansen, J E

AU - Nielsen, C M

AU - Nielsen, C

AU - Heegaard, P

AU - Mathiesen, Lars Reinhardt

AU - Nielsen, Jens Ole

PY - 1989

Y1 - 1989

N2 - The binding of 13 different lectins to gp120 partially purified from two HIV-1 isolates and one HIV-2 isolate was studied by in situ staining on electrophoretically separated and electroblotted HIV antigens. The lectins concanavalin A, wheat germ agglutinin, Lens culinaris agglutinin, Vicia faba agglutinin, Pisum sativum agglutinin and phytohaem(erythro)agglutinin bound to gp120 of all three isolates. The carbohydrate of gp120 recognized by lectins was thus arranged in at least four types of glycans: a high mannose type glycan, a bisected hybrid or complex type glycan, a biantennary fucosylated complex type glycan and a triantennary bisected complex type glycan. Only lectins which bound at least one of the four types of glycans were capable of inhibiting fusion of HIV-infected cells with CD4 cells by a carbohydrate-specific interaction with the HIV-infected cells. Thus, several different glycan structures may be implicated in CD4-gp120 binding.

AB - The binding of 13 different lectins to gp120 partially purified from two HIV-1 isolates and one HIV-2 isolate was studied by in situ staining on electrophoretically separated and electroblotted HIV antigens. The lectins concanavalin A, wheat germ agglutinin, Lens culinaris agglutinin, Vicia faba agglutinin, Pisum sativum agglutinin and phytohaem(erythro)agglutinin bound to gp120 of all three isolates. The carbohydrate of gp120 recognized by lectins was thus arranged in at least four types of glycans: a high mannose type glycan, a bisected hybrid or complex type glycan, a biantennary fucosylated complex type glycan and a triantennary bisected complex type glycan. Only lectins which bound at least one of the four types of glycans were capable of inhibiting fusion of HIV-infected cells with CD4 cells by a carbohydrate-specific interaction with the HIV-infected cells. Thus, several different glycan structures may be implicated in CD4-gp120 binding.

M3 - Journal article

VL - 3

SP - 635

EP - 641

JO - AIDS

JF - AIDS

SN - 1350-2840

IS - 10

ER -

ID: 34125611