EBV BMRF-2 facilitates cell-to-cell spread of virus within polarized oral epithelial cells
Abstract We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with β1 and αv family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2low recombinant v...
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| Published in | Virology (New York, N.Y.) Vol. 388; no. 2; pp. 335 - 343 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
05.06.2009
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| Subjects | |
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| Abstract | Abstract We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with β1 and αv family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2low recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells. |
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| AbstractList | Abstract We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with β1 and αv family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2low recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells. We previously reported that the Epstein-Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with b1 and av family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2 super(l) super(o) super(w) recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells. We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with β1 and αv family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2 low recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells. We previously reported that the Epstein-Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with β1 and αv family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2 low recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells. We previously reported that the Epstein-Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with beta1 and alphav family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2(low) recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells. |
| Author | Xiao, Jianqiao Tugizov, Sharof M Palefsky, Joel M Berline, Jennifer Herrera, Rossana |
| AuthorAffiliation | b Department of Orofacial Sciences, University of California, San Francisco, USA a Department of Medicine, University of California, San Francisco, USA |
| AuthorAffiliation_xml | – name: b Department of Orofacial Sciences, University of California, San Francisco, USA – name: a Department of Medicine, University of California, San Francisco, USA |
| Author_xml | – sequence: 1 fullname: Xiao, Jianqiao – sequence: 2 fullname: Palefsky, Joel M – sequence: 3 fullname: Herrera, Rossana – sequence: 4 fullname: Berline, Jennifer – sequence: 5 fullname: Tugizov, Sharof M |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19394065$$D View this record in MEDLINE/PubMed |
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| Snippet | Abstract We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by... We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by... We previously reported that the Epstein-Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by... |
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| SubjectTerms | Cell Line, Tumor EBV BMRF-2 EBV cell-to-cell spread Epithelial Cells - cytology Epithelial Cells - metabolism Epithelial Cells - virology Epstein-Barr virus Herpesvirus 4, Human - chemistry Herpesvirus 4, Human - genetics Herpesvirus 4, Human - physiology Humans Infectious Disease Lymphocytes - metabolism Lymphocytes - virology Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Mouth - cytology Mouth - virology Protein Sorting Signals Protein Transport Viral Proteins - genetics Viral Proteins - metabolism |
| Title | EBV BMRF-2 facilitates cell-to-cell spread of virus within polarized oral epithelial cells |
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