Identification of Human Junctional Adhesion Molecule 1 as a Functional Receptor for the Hom-1 Calicivirus on Human Cells

Sosnovtsev, Stanislav V.; Sandoval-Jaime, Carlos; Parra, Gabriel I.; Tin, Christine; Jones, Ronald W.; Soden, Jo; Barnes, Donna A.; Freeth, Jim; Smith, Alvin W.; Green, Kim Y.

doi:10.1128/mbio.00031-17

Cited by 23 publications

(20 citation statements)

References 51 publications

(89 reference statements)

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“…1 ). Feline calicivirus (FCV) and Hom-1 calicivirus employ junctional adhesion molecule A (JAM-A) and related proteins as receptors ( 36 , 37 ). The cryo-EM structure of the FCV capsid in complex with the two Ig-like extracellular domains of fJAM-A indicates this receptor also binds to the P2 subdomain, although the receptors appear to engage the top of the P domain near the dimer interface ( 38 ).…”

Section: Discussionmentioning

confidence: 99%

Structural basis for murine norovirus engagement of bile acids and the CD300lf receptor

Nelson

Wilen

Dai

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

211

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SignificanceThe mechanisms of norovirus capsid interactions with host receptors and the mechanisms by which soluble cofactors augment norovirus infection are not understood. We recently identified CD300lf as a cell surface receptor for murine norovirus (MNoV) and observed that a small molecule cofactor was critical for efficient binding of virus to CD300lf. Herein we identify the bile acid GCDCA as a cofactor enhancing MNoV infection and provide a biophysical characterization of the capsid–receptor and capsid–cofactor interactions, thereby providing a structure-based understanding of how noroviruses initiate cellular infection. This work has important implications for the design of norovirus therapeutics.

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Section: Discussionmentioning

confidence: 99%

Structural basis for murine norovirus engagement of bile acids and the CD300lf receptor

Nelson

Wilen

Dai

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

211

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“…Other powerful methods to be used in combination with glycomics and proteomics include RNA interference, CRISPR/Cas9 knockout, genome-wide haploid screens, cell-based arrays, drug-based approaches, and utilization of the microarray-characterized set of cells provided by US National Cancer Institute. We refer the reader elsewhere for further information on these methods [160][161][162][163][164][165][166]. A clear advantage of labelfree glycomics and proteomics technologies is, however, the minimal system perturbation in particular when untagged endogenous bait glycans and proteins are used.…”

Section: Alternative Approaches For Receptor Discoverymentioning

confidence: 99%

Glycomics and Proteomics Approaches to Investigate Early Adenovirus–Host Cell Interactions

Laßwitz

Chandra

Arnberg

2018

Journal of Molecular Biology

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Adenoviruses as most viruses rely on glycan and protein interactions to attach to and enter susceptible host cells. The Adenoviridae family comprises more than 80 human types and they differ in their attachment factor and receptor usage, which likely contributes to the diverse tropism of the different types. In the past years, methods to systematically identify glycan and protein interactions have advanced. In particular sensitivity, speed and coverage of mass spectrometric analyses allow for high-throughput identification of glycans and peptides separated by liquid chromatography. Also, developments in glycan microarray technologies have led to targeted, high-throughput screening and identification of glycan-based receptors. The mapping of cell surface interactions of the diverse adenovirus types has implications for cell, tissue, and species tropism as well as drug development. Here we review known adenovirus interactions with glycan- and protein-based receptors, as well as glycomics and proteomics strategies to identify yet elusive virus receptors and attachment factors. We finally discuss challenges, bottlenecks, and future research directions in the field of non-enveloped virus entry into host cells.

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“…Recently, it was observed that some HuNoVs and monkey recoviruses also utilize SAs as attachment factors ( 29 , 30 ). Finally, proteinaceous cellular surface structures were identified as receptors for a few caliciviruses, such as CD300lf and CD300ld for MNV ( 31 , 32 ) and junctional adhesion molecule-1 (JAM-1) for FCV and Hom-1 calicivirus ( 33 – 35 ).…”

Section: Introductionmentioning

confidence: 99%

Bovine Nebovirus Interacts with a Wide Spectrum of Histo-Blood Group Antigens

Cho

Soliman

Alfajaro

et al. 2018

J Virol

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Some viruses within the Caliciviridae family initiate their replication cycle by attachment to cell surface carbohydrate moieties, histo-blood group antigens (HBGAs), and/or terminal sialic acids (SAs). Although bovine nebovirus (BNeV), one of the enteric caliciviruses, is an important causative agent of acute gastroenteritis in cattle, its attachment factors and possibly other cellular receptors remain unknown. Using a comprehensive series of protein-ligand biochemical assays, we sought to determine whether BNeV recognizes cell surface HBGAs and/or SAs as attachment factors. It was found that BNeV virus-like particles (VLPs) bound to A type/H type 2/Ley HBGAs expressed in the bovine digestive tract and are related to HBGAs expressed in humans and other host species, suggesting a wide spectrum of HBGA recognition by BNeV. BNeV VLPs also bound to a large variety of different bovine and human saliva samples of all ABH and Lewis types, supporting previously obtained results and suggesting a zoonotic potential of BNeV transmission. Removal of α1,2-linked fucose and α1,3/4-linked fucose epitopes of target HBGAs by confirmation-specific enzymes reduced the binding of BNeV VLPs to synthetic HBGAs, bovine and human saliva, cultured cell lines, and bovine small intestine mucosa, further supporting a wide HBGA binding spectrum of BNeV through recognition of α1,2-linked fucose and α1,3/4-linked fucose epitopes of targeted HBGAs. However, removal of terminal α2,3- and α2,6-linked SAs by their specific enzyme had no inhibitory effects on binding of BNeV VLPs, indicating that BNeV does not use terminal SAs as attachment factors. Further details of the binding specificity of BNeV remain to be explored.IMPORTANCE Enteric caliciviruses such as noroviruses, sapoviruses, and recoviruses are the most important etiological agents of severe acute gastroenteritis in humans and many other mammalian host species. They initiate infection by attachment to cell surface carbohydrate moieties, HBGAs, and/or terminal SAs. However, the attachment factor(s) for BNeV, a recently classified enteric calicivirus genus/type species, remains unexplored. Here, we demonstrate that BNeV VLPs have a wide spectrum of binding to synthetic HBGAs, bovine and human saliva samples, and bovine duodenal sections. We further discovered that α1,2-linked fucose and α1,3/4-linked fucose epitopes are essential for binding of BNeV VLPs. However, BNeV VLPs do not bind to terminal SAs on cell carbohydrates. Continued investigation regarding the proteinaceous receptor(s) will be necessary for better understanding of the tropism, pathogenesis, and host range of this important viral genus.

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Identification of Human Junctional Adhesion Molecule 1 as a Functional Receptor for the Hom-1 Calicivirus on Human Cells

Cited by 23 publications

References 51 publications

Structural basis for murine norovirus engagement of bile acids and the CD300lf receptor

Structural basis for murine norovirus engagement of bile acids and the CD300lf receptor

Glycomics and Proteomics Approaches to Investigate Early Adenovirus–Host Cell Interactions

Bovine Nebovirus Interacts with a Wide Spectrum of Histo-Blood Group Antigens

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