Tags

Type your tag names separated by a space and hit enter

Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production.
Biochem Biophys Res Commun. 2009 Feb 06; 379(2):196-200.BB

Abstract

Dengue virus infection is an important mosquito-borne disease and a public health problem worldwide. A better understanding of interactions between human cellular host and dengue virus proteins will provide insight into dengue virus replication and cellular pathogenesis. The glycosylated envelope protein of dengue virus, DENV E, is processed in the endoplasmic reticulum of host cells and therefore reliant on host processing functions. The complement of host ER functions involved and nature of the interactions with DENV E has not been thoroughly investigated. By employing a yeast two-hybrid assay, we found that domain III of DENV E interacts with human immunoglobulin heavy chain binding protein (BiP). The relevance of this interaction was demonstrated by co-immunoprecipitation and co-localization of BiP and DENV E in dengue virus-infected cells. Using the same approach, association of DENV E with two other chaperones, calnexin and calreticulin was also observed. Knocking-down expression of BiP, calnexin, or calreticulin by siRNA significantly decreased the production of infectious dengue virions. These results indicate that the interaction of these three chaperones with DENV E plays an important role in virion production, likely facilitating proper folding and assembly of dengue proteins.

Authors+Show Affiliations

Department of Anatomy, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand. limjindaporn@yahoo.comNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19105951

Citation

Limjindaporn, Thawornchai, et al. "Interaction of Dengue Virus Envelope Protein With Endoplasmic Reticulum-resident Chaperones Facilitates Dengue Virus Production." Biochemical and Biophysical Research Communications, vol. 379, no. 2, 2009, pp. 196-200.
Limjindaporn T, Wongwiwat W, Noisakran S, et al. Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production. Biochem Biophys Res Commun. 2009;379(2):196-200.
Limjindaporn, T., Wongwiwat, W., Noisakran, S., Srisawat, C., Netsawang, J., Puttikhunt, C., Kasinrerk, W., Avirutnan, P., Thiemmeca, S., Sriburi, R., Sittisombut, N., Malasit, P., & Yenchitsomanus, P. T. (2009). Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production. Biochemical and Biophysical Research Communications, 379(2), 196-200. https://doi.org/10.1016/j.bbrc.2008.12.070
Limjindaporn T, et al. Interaction of Dengue Virus Envelope Protein With Endoplasmic Reticulum-resident Chaperones Facilitates Dengue Virus Production. Biochem Biophys Res Commun. 2009 Feb 6;379(2):196-200. PubMed PMID: 19105951.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production. AU - Limjindaporn,Thawornchai, AU - Wongwiwat,Wiyada, AU - Noisakran,Sansanee, AU - Srisawat,Chatchawan, AU - Netsawang,Janjuree, AU - Puttikhunt,Chunya, AU - Kasinrerk,Watchara, AU - Avirutnan,Panisadee, AU - Thiemmeca,Somchai, AU - Sriburi,Rungtawan, AU - Sittisombut,Nopporn, AU - Malasit,Prida, AU - Yenchitsomanus,Pa-thai, Y1 - 2008/12/25/ PY - 2008/11/19/received PY - 2008/12/08/accepted PY - 2008/12/25/entrez PY - 2008/12/25/pubmed PY - 2009/2/14/medline SP - 196 EP - 200 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 379 IS - 2 N2 - Dengue virus infection is an important mosquito-borne disease and a public health problem worldwide. A better understanding of interactions between human cellular host and dengue virus proteins will provide insight into dengue virus replication and cellular pathogenesis. The glycosylated envelope protein of dengue virus, DENV E, is processed in the endoplasmic reticulum of host cells and therefore reliant on host processing functions. The complement of host ER functions involved and nature of the interactions with DENV E has not been thoroughly investigated. By employing a yeast two-hybrid assay, we found that domain III of DENV E interacts with human immunoglobulin heavy chain binding protein (BiP). The relevance of this interaction was demonstrated by co-immunoprecipitation and co-localization of BiP and DENV E in dengue virus-infected cells. Using the same approach, association of DENV E with two other chaperones, calnexin and calreticulin was also observed. Knocking-down expression of BiP, calnexin, or calreticulin by siRNA significantly decreased the production of infectious dengue virions. These results indicate that the interaction of these three chaperones with DENV E plays an important role in virion production, likely facilitating proper folding and assembly of dengue proteins. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/19105951/Interaction_of_dengue_virus_envelope_protein_with_endoplasmic_reticulum_resident_chaperones_facilitates_dengue_virus_production_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(08)02402-9 DB - PRIME DP - Unbound Medicine ER -