TY - JOUR
T1 - The Astounding World of Glycans from Giant Viruses
AU - Speciale, Immacolata
AU - Notaro, Anna
AU - Abergel, Chantal
AU - Lanzetta, Rosa
AU - Lowary, Todd L.
AU - Molinaro, Antonio
AU - Tonetti, Michela
AU - Van Etten, James L.
AU - De Castro, Cristina
N1 - Funding Information:
C.D.C. gratefully acknowledges STARPLUS 2020 (project no. 21-UNINA-EPIG-042) and FRA promoted from the University of Napoli for financial support. A.N. acknowledges UIF Vinci program 2015 (contract C3_90) and 2019 (contract C4-180), and STAR2-2017 project for financial support. C.A. acknowledges the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (grant agreement no. 832601) for financial support. T.L.L. gratefully acknowledges Academia Sinica for financial support. The chlorovirus research in the Van Etten lab has been supported by grants from the National Institutes of Health, the National Science Foundation, the United States Dept of Agriculture, the United States Department of Energy, and the University of Nebraska over the past 40 years. Current support is provided by the National Science Foundation under grant no. 1736030. The authors apologize to the many colleagues who have influenced their thinking through work that was not explicitly cited in this review.
Publisher Copyright:
© 2022 American Chemical Society. All rights reserved.
PY - 2022/10/26
Y1 - 2022/10/26
N2 - Viruses are a heterogeneous ensemble of entities, all sharing the need for a suitable host to replicate. They are extremely diverse, varying in morphology, size, nature, and complexity of their genomic content. Typically, viruses use host-encoded glycosyltransferases and glycosidases to add and remove sugar residues from their glycoproteins. Thus, the structure of the glycans on the viral proteins have, to date, typically been considered to mimick those of the host. However, the more recently discovered large and giant viruses differ from this paradigm. At least some of these viruses code for an (almost) autonomous glycosylation pathway. These viral genes include those that encode the production of activated sugars, glycosyltransferases, and other enzymes able to manipulate sugars at various levels. This review focuses on large and giant viruses that produce carbohydrate-processing enzymes. A brief description of those harboring these features at the genomic level will be discussed, followed by the achievements reached with regard to the elucidation of the glycan structures, the activity of the proteins able to manipulate sugars, and the organic synthesis of some of these virus-encoded glycans. During this progression, we will also comment on many of the challenging questions on this subject that remain to be addressed.
AB - Viruses are a heterogeneous ensemble of entities, all sharing the need for a suitable host to replicate. They are extremely diverse, varying in morphology, size, nature, and complexity of their genomic content. Typically, viruses use host-encoded glycosyltransferases and glycosidases to add and remove sugar residues from their glycoproteins. Thus, the structure of the glycans on the viral proteins have, to date, typically been considered to mimick those of the host. However, the more recently discovered large and giant viruses differ from this paradigm. At least some of these viruses code for an (almost) autonomous glycosylation pathway. These viral genes include those that encode the production of activated sugars, glycosyltransferases, and other enzymes able to manipulate sugars at various levels. This review focuses on large and giant viruses that produce carbohydrate-processing enzymes. A brief description of those harboring these features at the genomic level will be discussed, followed by the achievements reached with regard to the elucidation of the glycan structures, the activity of the proteins able to manipulate sugars, and the organic synthesis of some of these virus-encoded glycans. During this progression, we will also comment on many of the challenging questions on this subject that remain to be addressed.
UR - http://www.scopus.com/inward/record.url?scp=85135193945&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85135193945&partnerID=8YFLogxK
U2 - 10.1021/acs.chemrev.2c00118
DO - 10.1021/acs.chemrev.2c00118
M3 - Review article
C2 - 35820164
AN - SCOPUS:85135193945
VL - 122
SP - 15717
EP - 15766
JO - Chemical Reviews
JF - Chemical Reviews
SN - 0009-2665
IS - 20
ER -