Recruitment of Nectin-3 to Cell-Cell Junctions through trans-Heterophilic Interaction with CD155, a Vitronectin and Poliovirus Receptor That Localizes to αvβ3 Integrin-containing Membrane Microdomains
Open accessAbstract
Nectins present a novel class of Ig superfamily adhesion molecules that, cooperatively with cadherins, establish and maintain cell-cell adherens junctions. CD155, the cognate receptor for poliovirus, undergoes cell-matrix contacts by binding to the extracellular matrix protein vitronectin. The significant homology of nectins with CD155 prompted us to investigate the possibility of their interaction. We determined that nectin-3 binds CD155 and its putative mouse homologue Tage4 in cell-based ligand binding assays. Coculture of nectin-3- and CD155-expressing HeLa cells led to CD155-dependent recruitment of nectin-3 to cell-cell contacts. In a heterologous coculture system with CD155 expressing mouse neuroblastoma cells, HeLa cell-expressed nectin-3 was recruited to contact sites with CD155 bearing neurites. CD155 and nectin-3 colocalized to epithelial cell-cell junctions in renal proximal tubules and in the amniotic membrane. Efficient interaction depended on CD155 dimerization, which appears to be aided by cell type-specific cofactors. We furthermore found CD155 to codistribute with alpha(v) integrin microdomains on the surface of transfected mouse fibroblasts and at amniotic epithelial cell junctions. Our findings demonstrate the possible trans-interaction between the bona fide cell-cell adherens type adhesion system (cadherin/nectin) and the cell-matrix adhesion system (integrin/CD155) by virtue of their nectin-3 and CD155 components, respectively.
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Substitutions in the IRES contribute most to the attenuated phenotype of the Sabin 1 and Sabin 3 strains.
“The substitutions in the IRES, which alter stem-loop structures (63, 68, 126, 132) and reduce the efficiency of initiation of translation of the poliovirus RNA template (68, 188), contribute most to the attenuated phenotype of the Sabin 1 and Sabin 3 strains.”
From VACCINE-DERIVED POLIOVIRUSES AND THE ENDGAME STRATEGY FOR GLOBAL POLIO ERADICATION (2005) · cites this paper as [132]
Mutations that restore the original stem-loop structure in the IRES are frequently found in vaccine-related isolates from healthy OPV recipients, patients with VAPP, and the environment.
“Mutations that restore the original stem-loop structure in the IRES [Sabin 1: G480A (backmutation) or U525C (suppressor); Sabin 2: A481G;Sabin3:U472C]arefrequentlyfound in vaccine-related isolates from healthy OPV recipients (127, 132) and patients with VAPP (61), as well as from the environment (228).”
From VACCINE-DERIVED POLIOVIRUSES AND THE ENDGAME STRATEGY FOR GLOBAL POLIO ERADICATION (2005) · cites this paper as [132]
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- Authors
- Mueller, S., & Wimmer, E.
- Affiliations
- Stony Brook University (US)
- Corresponding author
- Wimmer, Eckard
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-08
- Volume
- 278
- Issue
- 33
- Pages
- 31251-31260
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1980311792
- Cited by
- 90
- References
- 56
- Citations by year
- 2024: 2 · 2023: 1 · 2022: 5 · 2021: 1 · 2020: 4 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 4 · 2015: 1 · 2014: 2 · 2013: 6 · 2012: 6
- FWCI
- 4.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI-39485)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- nectin-3, CD155, integrin αvβ3, poliovirus receptor, cell-cell contact, adherens junctions, alpha v beta 3 integrin, lipid rafts, trans-interactions, epithelial cell adhesion, amniotic membrane, proximal tubule
- MeSH terms
- Nectins, Amnion, Animals, Antigens, Neoplasm, Cell Adhesion, Cell Communication, Epithelial Cells, Fibroblasts, HeLa Cells, Humans, Intercellular Junctions, Kidney, Ligands, Membrane Proteins, Neoplasm Proteins, Neuroblastoma, Receptors, Cell Surface, Receptors, Virus, Cell Adhesion Molecules, PC12 Cells, Protein Structure, Tertiary, Dimerization, COS Cells, Integrin alphaVbeta3, Mice, Rats
About these checks
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