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Curr HIV/AIDS Rep. 2019 Apr;16(2):151-168. doi: 10.1007/s11904-019-00433-w.

Breaking the Glyco-Code of HIV Persistence and Immunopathogenesis.

Author information

1
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA, USA.
2
Genos Glycoscience Research Laboratory, Borongajska cesta 83h, Zagreb, Croatia.
3
Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovacica 1, Zagreb, Croatia.
4
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA, USA. mmohsen@wistar.org.

Abstract

PURPOSE OF REVIEW:

Glycoimmunology is an emerging field focused on understanding how immune responses are mediated by glycans (carbohydrates) and their interaction with glycan-binding proteins called lectins. How glycans influence immunological functions is increasingly well understood. In a parallel way, in the HIV field, it is increasingly understood how the host immune system controls HIV persistence and immunopathogenesis. However, what has mostly been overlooked, despite its potential for therapeutic applications, is the role that the host glycosylation machinery plays in modulating the persistence and immunopathogenesis of HIV. Here, we will survey four areas in which the links between glycan-lectin interactions and immunology and between immunology and HIV are well described. For each area, we will describe these links and then delineate the opportunities for the HIV field in investigating potential interactions between glycoimmunology and HIV persistence/immunopathogenesis.

RECENT FINDINGS:

Recent studies show that the human glycome (the repertoire of human glycan structures) plays critical roles in driving or modulating several cellular processes and immunological functions that are central to maintaining HIV infection. Understanding the links between glycoimmunology and HIV infection may create a new paradigm for discovering novel glycan-based therapies that can lead to eradication, functional cure, or improved tolerance of lifelong infection.

KEYWORDS:

Fucosylation; Galactosylation; Galectins; Glycosylation; HIV persistence; Sialylation

PMID:
30707400
PMCID:
PMC6441623
[Available on 2020-04-01]
DOI:
10.1007/s11904-019-00433-w

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