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Review
. 2019 Oct 22:7:710.
doi: 10.3389/fchem.2019.00710. eCollection 2019.

Mucins and Pathogenic Mucin-Like Molecules Are Immunomodulators During Infection and Targets for Diagnostics and Vaccines

Affiliations
Review

Mucins and Pathogenic Mucin-Like Molecules Are Immunomodulators During Infection and Targets for Diagnostics and Vaccines

Sandra Pinzón Martín et al. Front Chem. .

Erratum in

Abstract

Mucins and mucin-like molecules are highly O-glycosylated proteins present on the cell surface of mammals and other organisms. These glycoproteins are highly diverse in the apoprotein and glycan cores and play a central role in many biological processes and diseases. Mucins are the most abundant macromolecules in mucus and are responsible for its biochemical and biophysical properties. Mucin-like molecules cover various protozoan parasites, fungi and viruses. In humans, modifications in mucin glycosylation are associated with tumors in epithelial tissue. These modifications allow the distinction between normal and abnormal cell conditions and represent important targets for vaccine development against some cancers. Mucins and mucin-like molecules derived from pathogens are potential diagnostic markers and targets for therapeutic agents. In this review, we summarize the distribution, structure, role as immunomodulators, and the correlation of human mucins with diseases and perform a comparative analysis of mucins with mucin-like molecules present in human pathogens. Furthermore, we review the methods to produce pathogenic and human mucins using chemical synthesis and expression systems. Finally, we present applications of mucin-like molecules in diagnosis and prevention of relevant human diseases.

Keywords: O-glycoproteins; cancer; infection; mucin-like molecules; mucins; parasites; virus.

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Figures

Figure 1
Figure 1
Structure of human mucin glycans. (A) Schematic and chemical representation of the organization of mucins glycans, (B) Structure of the glycan cores present in mucins.
Figure 2
Figure 2
Schematic representation of the structure from secreted-gel-forming, secreted-non-gel forming and transmembrane human mucins.
Figure 3
Figure 3
Variation of the protein-glycan and membrane linkage and glycan structures in human mucins and protozoan MLMs.
Figure 4
Figure 4
Chemical structure of synthesized glycans from MLMs of Trypanosoma cruzi Colombiana strain (18) and Y strain (913).

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