Recognition of human immunodeficiency virus glycoproteins by natural anti-carbohydrate antibodies in human serum

Takami Tomiyama; Douglas Lake; Yasuhiko Masuho; Evan M. Hersh

doi:10.1016/0006-291X(91)91979-M

Recognition of human immunodeficiency virus glycoproteins by natural anti-carbohydrate antibodies in human serum

Takami Tomiyama, Douglas Lake, Yasuhiko Masuho, Evan M. Hersh

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Anti-carbohydrate antibodies were isolated from Human immunodeficiency virus (HIV) negative human serum by affinity chromatography using yeast mannan followed by protein A. The purified mannan-binding IgG (MBIgG) bound to HIV glycoproteins gp160, gp120 and gp41 in Western blot. Immunofluorescence revealed that MBIgG bound to HIV IIIB-infected H9 cells but not to uninfected H9 cells, suggesting that carbohydrate structures recognized by MBIgG are specifically expressed on HIV-infected cells. MBIgG did not neutralize infectivity of HIV. These results show that normal human serum contains natural antibodies reactive to carbohydrate structures of HIV glycoproteins propagated in human cells.

Original language	English (US)
Pages (from-to)	279-285
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	177
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(91)91979-M
State	Published - May 31 1991
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(91)91979-M

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title = "Recognition of human immunodeficiency virus glycoproteins by natural anti-carbohydrate antibodies in human serum",

abstract = "Anti-carbohydrate antibodies were isolated from Human immunodeficiency virus (HIV) negative human serum by affinity chromatography using yeast mannan followed by protein A. The purified mannan-binding IgG (MBIgG) bound to HIV glycoproteins gp160, gp120 and gp41 in Western blot. Immunofluorescence revealed that MBIgG bound to HIV IIIB-infected H9 cells but not to uninfected H9 cells, suggesting that carbohydrate structures recognized by MBIgG are specifically expressed on HIV-infected cells. MBIgG did not neutralize infectivity of HIV. These results show that normal human serum contains natural antibodies reactive to carbohydrate structures of HIV glycoproteins propagated in human cells.",

author = "Takami Tomiyama and Douglas Lake and Yasuhiko Masuho and Hersh, {Evan M.}",

note = "Funding Information: We thank Dr. JosephU termohlen and Dr. Takashi Kawamura for helpful advice and discussions. This work was supported by Teijin Limited, Tokyo, Japanand a grant from the NIAID, NM, Bethesda,M D.",

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AU - Lake, Douglas

AU - Masuho, Yasuhiko

AU - Hersh, Evan M.

N1 - Funding Information: We thank Dr. JosephU termohlen and Dr. Takashi Kawamura for helpful advice and discussions. This work was supported by Teijin Limited, Tokyo, Japanand a grant from the NIAID, NM, Bethesda,M D.

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AB - Anti-carbohydrate antibodies were isolated from Human immunodeficiency virus (HIV) negative human serum by affinity chromatography using yeast mannan followed by protein A. The purified mannan-binding IgG (MBIgG) bound to HIV glycoproteins gp160, gp120 and gp41 in Western blot. Immunofluorescence revealed that MBIgG bound to HIV IIIB-infected H9 cells but not to uninfected H9 cells, suggesting that carbohydrate structures recognized by MBIgG are specifically expressed on HIV-infected cells. MBIgG did not neutralize infectivity of HIV. These results show that normal human serum contains natural antibodies reactive to carbohydrate structures of HIV glycoproteins propagated in human cells.

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Recognition of human immunodeficiency virus glycoproteins by natural anti-carbohydrate antibodies in human serum

Abstract

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