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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Expression and purification of human respiratory syncytial virus recombinant fusion protein

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Author(s):
Arcuri, Helen A. [1] ; Apponi, Luciano H. [2] ; Valentini, Sandro R. [2] ; Durigon, Edison L. [3] ; de Azevedo, Walter F. [4] ; Fossey, Marcelo A. [1] ; Rahal, Paula [1] ; de Souza, Fatima P. [1]
Total Authors: 8
Affiliation:
[1] UNESP, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[2] UNESP, Fac Ciencias Farmaceut, BR-14801902 Araraquara, SP - Brazil
[3] Univ Sao Paulo, Inst Ciencias Biomed, BR-05508900 Sao Paulo - Brazil
[4] PUCRGS, Fac Ciencias Biol, BR-90619900 Porto Alegre, RS - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Protein Expression and Purification; v. 62, n. 2, p. 146-152, DEC 2008.
Web of Science Citations: 1
Abstract

The Human Respiratory Syncytial Virus (HRSV) fusion protein (F) was expressed in Escherichia call BL21A using the pET28a vector at 37 degrees C. The protein was purified from the soluble fraction using affinity resin. The structural quality of the recombinant fusion protein and the estimation of its secondary structure were obtained by circular dichroism. Structural models of the fusion protein presented 46% of the helices in agreement with the spectra by circular dichroism analysis. There are only few studies that succeeded in expressing the HRSV fusion protein in bacteria. This is a report on human fusion protein expression in E. call and structure analysis, representing a step forward in the development of fusion protein F inhibitors and the production of antibodies. (c) 2008 Elsevier Inc. All rights reserved. (AU)