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Updated: Aug 16, 2026
Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line
Published on: September 28, 2022
Identification of three gp350/220 regions involved in Epstein-Barr virus invasion of host cells
Mauricio Urquiza1, Ramses Lopez, Helena Patiño
1Fundación Instituto de Inmunología de Colombia, Bogotá 030405, Colombia. mauricio_urquiza@fidic.org.co
Abstract:
Epstein-Barr virus (EBV) invasion of B-lymphocytes involves EBV gp350/220 binding to B-lymphocyte CR2. The anti-gp350 monoclonal antibody (mAb)-72A1 Fab inhibits this binding and therefore blocks EBV invasion of target cells. However, gp350/220 regions interacting with mAb 72A1 and involved in EBV invasion of target cells have not yet been identified. This work reports three gp350/220 regions, defined by peptide 11382, 11389, and 11416 sequences, that are involved in EBV binding to B-lymphocytes. Peptides 11382, 11389, and 11416 bound to CR2(+) but not to CR2(-) cells, inhibited EBV invasion of cord blood lymphocytes (CBLs), were recognized by mAb 72A1, and inhibited mAb 72A1 binding to EBV. Peptides 11382 and 11416 binding to peripheral blood lymphocytes (PBLs) induced interleukin-6 protein synthesis in these cells, this phenomenon being inhibited by mAb 72A1. The same behavior has been reported for gp350/220 binding to PBLs. Anti-peptide 11382, 11389, and 11416 antibodies inhibited EBV binding and EBV invasion of PBLs and CBLs. Peptide 11382, 11389, and 11416 sequences presented homology with the C3dg regions coming into contact with CR2 (C3dg and gp350 bound to similar CR2 regions). These peptides could be used in designing strategies against EBV infection.
Insights
Researchers identified three specific regions on Epstein-Barr virus (EBV) gp350/220 that are crucial for binding to B-lymphocytes. These identified peptides offer potential targets for developing new strategies to combat EBV infection.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Epstein-Barr virus (EBV) infects B-lymphocytes by binding its gp350/220 envelope protein to the CR2 receptor on these cells.
- Monoclonal antibody (mAb)-72A1 Fab fragments inhibit EBV entry by blocking gp350/220 binding to CR2, but the specific interaction sites were unknown.
Purpose of the Study:
- To identify the specific regions of EBV gp350/220 that mediate binding to B-lymphocytes and interact with mAb 72A1.
- To investigate the functional role of these identified regions in EBV invasion and B-cell activation.
Main Methods:
- Synthesis and characterization of peptides representing specific sequences of EBV gp350/220 (peptides 11382, 11389, and 11416).
- Assays to evaluate peptide binding to CR2-positive and CR2-negative cells.
- Inhibition assays to assess the effect of peptides and anti-peptide antibodies on EBV binding and invasion of lymphocytes (CBLs and PBLs).
- Analysis of interleukin-6 (IL-6) protein synthesis induced by peptide binding to peripheral blood lymphocytes (PBLs).
- Bioinformatic analysis to identify homologies between peptide sequences and complement C3dg regions interacting with CR2.
Main Results:
- Peptides 11382, 11389, and 11416 specifically bound to CR2(+) cells and inhibited EBV invasion of cord blood lymphocytes (CBLs).
- These peptides were recognized by mAb 72A1 and inhibited the binding of mAb 72A1 to EBV.
- Peptides 11382 and 11416 induced IL-6 synthesis in peripheral blood lymphocytes (PBLs), a response also inhibited by mAb 72A1.
- Anti-peptide antibodies targeting these sequences effectively blocked EBV binding and invasion of both CBLs and PBLs.
- Sequence homology analysis revealed that peptides 11382, 11389, and 11416 share similarities with C3dg regions that bind to CR2.
Conclusions:
- Three distinct regions within EBV gp350/220 (peptides 11382, 11389, 11416) are critical for CR2-mediated B-lymphocyte binding and EBV entry.
- These identified peptides represent key functional domains involved in EBV-CR2 interactions and are recognized by the inhibitory mAb 72A1.
- The findings suggest that these peptide sequences can be utilized as targets for developing novel therapeutic strategies against EBV infection.
