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Two Epstein-Barr virus glycoprotein complexes.
Hutt-Fletcher LM, Lake CM. Hutt-Fletcher LM, et al. Curr Top Microbiol Immunol. 2001;258:51-64. doi: 10.1007/978-3-642-56515-1_4. Curr Top Microbiol Immunol. 2001. PMID: 11443867 Review. No abstract available.
Virus isolation.
Hutt-Fletcher LM, Turk SM. Hutt-Fletcher LM, et al. Methods Mol Biol. 2001;174:119-23. doi: 10.1385/1-59259-227-9:119. Methods Mol Biol. 2001. PMID: 11357633 No abstract available.
Epstein-Barr virus shed in saliva is high in B-cell-tropic glycoprotein gp42.
Jiang R, Scott RS, Hutt-Fletcher LM. Jiang R, et al. J Virol. 2006 Jul;80(14):7281-3. doi: 10.1128/JVI.00497-06. J Virol. 2006. PMID: 16809335 Free PMC article.
Epstein-Barr virus gH is essential for penetration of B cells but also plays a role in attachment of virus to epithelial cells.
Molesworth SJ, Lake CM, Borza CM, Turk SM, Hutt-Fletcher LM. Molesworth SJ, et al. J Virol. 2000 Jul;74(14):6324-32. doi: 10.1128/jvi.74.14.6324-6332.2000. J Virol. 2000. PMID: 10864642 Free PMC article.
The Epstein-Barr virus (EBV) gN homolog BLRF1 encodes a 15-kilodalton glycoprotein that cannot be authentically processed unless it is coexpressed with the EBV gM homolog BBRF3.
Lake CM, Molesworth SJ, Hutt-Fletcher LM. Lake CM, et al. J Virol. 1998 Jul;72(7):5559-64. doi: 10.1128/JVI.72.7.5559-5564.1998. J Virol. 1998. PMID: 9621013 Free PMC article.
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