2007
DOI: 10.1128/jvi.01509-07
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Identification of Regions and Residues in Feline Junctional Adhesion Molecule Required for Feline Calicivirus Binding and Infection

Abstract: The feline junctional adhesion molecule A (fJAM-A) is a functional receptor for feline calicivirus (FCV).fJAM-A is a member of the immunoglobulin superfamily (IgSF) and consists of two Ig-like extracellular domains (D1 and D2), a membrane-spanning domain, and a short cytoplasmic tail. To identify regions of fJAM-A that interact with FCV, we purified recombinant fJAM-A ectodomain and D1 and D2 domains. We found that preincubation of FCV with the ectodomain or D1 was sufficient to inhibit FCV infection in plaque… Show more

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Cited by 39 publications
(56 citation statements)
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“…Docking homology models to our reconstruction led to the synthesis of a quasiatomic-resolution model of the interaction, allowing us to establish a putative footprint of contact residues on both VP1 and fJAM-A and showing that FCV binds primarily to the membrane-proximal D1 domain of fJAM-A. These findings were consistent with those of published mutagenesis experiments indicating that D1 was the most important domain for FCV binding and highlighting three residues in fJAM-A (D42, K43, and S97) that play a key role in FCV attachment (18).…”
supporting
confidence: 80%
See 1 more Smart Citation
“…Docking homology models to our reconstruction led to the synthesis of a quasiatomic-resolution model of the interaction, allowing us to establish a putative footprint of contact residues on both VP1 and fJAM-A and showing that FCV binds primarily to the membrane-proximal D1 domain of fJAM-A. These findings were consistent with those of published mutagenesis experiments indicating that D1 was the most important domain for FCV binding and highlighting three residues in fJAM-A (D42, K43, and S97) that play a key role in FCV attachment (18).…”
supporting
confidence: 80%
“…Ossiboff and Parker have identified three amino acid residues, mutation of which led to reductions in binding to FCV strain 5: D42, K43, and S97 (18). In their initial study describing fJAM-A as the functional receptor for FCV, Makino et al (15) proposed that S91 and K155 may also be important, following comparison of sequences for fJAM-A and simian JAM-A (which bind FCV) with human JAM-A (which does not).…”
Section: Figmentioning
confidence: 99%
“…Domain deletion and mutagenesis experiments have mapped the virus interactions to outermost D1 domain (Ossiboff and Parker 2007). It is interesting to note that bacterially expressed fJAM-1, which is devoid of any glycan modifications, is able to inhibit virus binding to cells (Ossiboff and Parker 2007). This would suggest that the sialic acid on fJAM-1 is not necessary for binding of the receptor to FCV.…”
Section: Feline Calicivirus Interactions With Its Receptormentioning
confidence: 96%
“…JAM-1 is a member of the immunoglobulin-like superfamily of proteins found on the surface of leukocytes and blood platelets and is thought to regulate the formation of tight junctions in epithelial and endothelial cells. Domain deletion and mutagenesis experiments have mapped the virus interactions to outermost D1 domain (Ossiboff and Parker 2007). It is interesting to note that bacterially expressed fJAM-1, which is devoid of any glycan modifications, is able to inhibit virus binding to cells (Ossiboff and Parker 2007).…”
Section: Feline Calicivirus Interactions With Its Receptormentioning
confidence: 99%
“…Several papers 17,18 have described the feline junctional adhesion molecule 1 (fjAM-1) as being important to calicivirus infection. These were produced from RNA of Crandell Reese feline kidney cells and amplified by reverse transcription PCR.…”
Section: Tem Investigations Of Adhesion Mechanismmentioning
confidence: 99%