Expression, Purification and Characterization of Hiv-1 Capsid Precursor Protein P41

Overview

Journal Protein J

Publisher Springer

Specialty Biochemistry

Date 2018 Mar 7

PMID 29508209

Authors

Zhiqing Zhang

Lei Wang

Shimeng Bai

Jiaming Qiao

Honglin Shen

Fang Huang

Shuangquan Gao

Shaoyong Li

Shaowei Li

Ying Gu

Ningshao Xia

Affiliations

Soon will be listed here.

Abstract

Human immunodeficiency virus type 1 (HIV-1) has been a global epidemic since 1983; yet, the virology and immunology related to HIV-1 remain elusive. Furthermore, as there is still no effective chemoprophylaxis or vaccine to treat patients with HIV-1, most research focuses on strategies to prevent HIV-1 infection, such as with antiviral drugs, novel therapeutics, or improved diagnostic kits. The HIV-1 Gag precursor protein (p55)-comprising the matrix (MA/p17), capsid (CA/p24), and nucleocapsid (NC/p7) protein domains-is the main structural HIV-1 protein, and is uniquely responsible for virion assembly within the virus life cycle. Recently, the immature and mature capsid structures were solved; however, the precursor protein structure is still unknown. Here, we expressed two subtypes of HIV-1 MA-CA stretch of the Gag protein, referred to as p41, in a bacterial expression system. We characterized the purified p41 protein, and showed its superior antigenicity over that of p24, highlighting the potential influence of the p17 domain on p24 structure. We further showed that p41 has good immunogenicity to induce an antibody response in mice. These results will aid future investigations into the HIV-1 capsid precursor structure, and potentially contribute to improving the design of diagnostic kits.

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