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1.
Arch Virol ; 169(8): 167, 2024 Jul 17.
Article in English | MEDLINE | ID: mdl-39020055

ABSTRACT

Epstein‒Barr virus (EBV) is a double-stranded DNA virus belonging to the family Orthoherpesviridae that is associated with the development of various tumors, such as lymphoma, nasopharyngeal carcinoma, and gastric cancer. There are no uniformly effective treatments for human EBV infection, and vaccines and immunotherapies are currently the main research directions. The glycoproteins gB and gH/gL are surface glycoproteins that are common to all herpesviruses, with subtle differences in structure and function between different viruses. The core membrane fusion machinery constituted by EBV gB and gH/gL is an important target of neutralizing antibodies in epithelial EBV infection due to its essential role in the fusion of viral and target cell membranes. In this article, we review the main modes of EBV infection, the structure and function of the core fusion machinery gB and gH/gL, and the development of neutralizing antibodies and prophylactic vaccines based on this target.


Subject(s)
Antibodies, Neutralizing , Epstein-Barr Virus Infections , Herpesvirus 4, Human , Viral Envelope Proteins , Humans , Epstein-Barr Virus Infections/prevention & control , Epstein-Barr Virus Infections/immunology , Epstein-Barr Virus Infections/virology , Antibodies, Neutralizing/immunology , Herpesvirus 4, Human/immunology , Herpesvirus 4, Human/genetics , Viral Envelope Proteins/immunology , Viral Envelope Proteins/genetics , Antibodies, Viral/immunology , Virus Internalization , Animals , Viral Vaccines/immunology , Viral Proteins/immunology , Viral Proteins/genetics , Membrane Glycoproteins , Molecular Chaperones
2.
Pathol Res Pract ; 260: 155427, 2024 Jun 24.
Article in English | MEDLINE | ID: mdl-38936091

ABSTRACT

Nasopharyngeal carcinoma (NPC) is closely related to Epstein-Barr virus (EBV) infection, and glycosylation of proteins is associated with precancerous lesions and carcinogenesis of NPC, and viral glycoproteins mediates the fusion of viruses with B cells or epithelial cells in the infection stage, promoting the conversion of normal epithelial cells into cancer cells. In the process of occurrence and development of NPC, various glycoproteins in the body promote or inhibit the proliferation, invasion, metastasis, and drug resistance of tumor cells, such as the tumor inhibitory effect of NGX6 and inhibin B (INHBB); the cancer-promoting effect of tenascin-C (TNC), fibronectin 1 (FN1), insulin-like growth factor binding protein-3 (IGFBP3), serglycin, and its core protein; and some effects of glycosylation of immune proteins on immunotherapy in NPC. This article provides an overview of the research progress on the interaction of glycoproteins associated with EBV infection with the occurrence and development of NPC.

3.
Biomolecules ; 12(12)2022 11 23.
Article in English | MEDLINE | ID: mdl-36551160

ABSTRACT

The core-1 ß1-3galactosyltransferase-specific chaperone 1 (Cosmc) is a unique molecular chaperone of core-1 ß1-3galactosyltransferase(C1GALT1), which typically functions inside the endoplasmic reticulum (ER). Cosmc helps C1GALT1 to fold correctly and maintain activity. It also participates in the synthesis of the T antigen, O-glycan, together with C1GALT1. Cosmc is a multifaceted molecule with a wide range of roles and functions. It involves platelet production and the regulation of immune cell function. Besides that, the loss of function of Cosmc also facilitates the development of several diseases, such as inflammation diseases, immune-mediated diseases, and cancer. It suggests that Cosmc is a critical control point in diseases and that it should be regarded as a potential target for oncotherapy. It is essential to fully comprehend Cosmc's roles, as they may provide critical information about its involvement in disease development and pathogenesis. In this review, we summarize the recent progress in understanding the role of Cosmc in normal development and diseases.


Subject(s)
Disease , Molecular Chaperones , Humans , Endoplasmic Reticulum/metabolism , Molecular Chaperones/metabolism , Glycosylation
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