对在表面环上工程化带有HIV-gp41表位的伤寒沙门氏菌OmpC和OmpF孔蛋白的特性分析

Characterization of Salmonella typhi OmpC and OmpF porins engineered with HIV-gp41 epitope on the surface loops.

作者信息

Thulasingam Madhuranayaki, Damodharan Subha, Madhana Vigneshwari Gopal, P J Pandaranayaka Eswari, Elizabeth Hanna Luke, Usha Ramakrishnan, Krishnaswamy Sankaran

机构信息

School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.

National Institute for Research in Tuberculosis, Indian Council of Medical Research, Chennai, 600031, India.

出版信息

Proteins. 2017 Apr;85(4):657-664. doi: 10.1002/prot.25246. Epub 2017 Feb 3.

DOI:10.1002/prot.25246

PMID:28076882

Abstract

Porins form trimers in the outer membrane and help transport nutrients and waste products across the bacterial cell membrane. Porin loops are suitable candidates as display systems due to their high immunogenicity and presentation at the bacterial cell surface. In this study, Salmonella typhi porins (OmpC and OmpF) engineered with the Kennedy peptide from gp41 of HIV were characterised. The chimeric OmpC carrying the Kennedy peptide in loop7 did not trimerise, whereas the chimeric OmpF with the epitope in loop5 formed trimers and also was recognised by the antibodies in the HIV patient serum. The results suggest that chimeric S. typhi OmpF may be taken further as a potential candidate to develop as an epitope display system. Proteins 2017; 85:657-664. © 2016 Wiley Periodicals, Inc.

摘要

孔蛋白在外膜中形成三聚体，有助于营养物质和代谢废物跨细菌细胞膜运输。由于孔蛋白环具有高免疫原性且呈现在细菌细胞表面，因此是作为展示系统的合适候选者。在本研究中，对用来自HIV gp41的肯尼迪肽工程改造的伤寒沙门氏菌孔蛋白（OmpC和OmpF）进行了表征。在环7携带肯尼迪肽的嵌合OmpC没有三聚化，而在环5带有表位的嵌合OmpF形成了三聚体，并且也被HIV患者血清中的抗体识别。结果表明，嵌合伤寒沙门氏菌OmpF可能作为潜在候选者进一步开发成为一种表位展示系统。《蛋白质》2017年；85:657 - 664。©2016威利期刊公司。