Literature DB >> 12077458

Crystallization and preliminary structural analysis of an antibody complex formed with PfMSP1-19, a malaria vaccine candidate.

J C Pizarro1, V Chitarra, C Calvet, D Verger, G A Bentley.   

Abstract

The 11 kDa C-terminal fragment of the proteolyticly matured surface antigen, PfMSP1, from Plasmodium falciparum is a promising malaria vaccine candidate. The soluble recombinant form of this naturally occurring fragment has been crystallized as a complex with the Fab of a specific murine monoclonal antibody. The crystals belong to the space group P2(1), with unit-cell parameters a = 51.8, b = 213.5,c = 60.0 A, beta =101.0 degrees, and with Z = 4. Diffraction data have been measured to 2.9 A resolution and a preliminary model of the complex has been determined by molecular replacement. The epitope recognised by G17.12 is located on the N-terminal EGF-like domain of the antigen.

Entities:  

Mesh:

Substances:

Year:  2002        PMID: 12077458     DOI: 10.1107/s0907444902007667

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Genetic linkage of autologous T cell epitopes in a chimeric recombinant construct improves anti-parasite and anti-disease protective effect of a malaria vaccine candidate.

Authors:  Balwan Singh; Monica Cabrera-Mora; Jianlin Jiang; Mary Galinski; Alberto Moreno
Journal:  Vaccine       Date:  2010-01-22       Impact factor: 3.641

2.  Neutralizing and interfering human antibodies define the structural and mechanistic basis for antigenic diversion.

Authors:  Palak N Patel; Thayne H Dickey; Christine S Hopp; Ababacar Diouf; Wai Kwan Tang; Carole A Long; Kazutoyo Miura; Peter D Crompton; Niraj H Tolia
Journal:  Nat Commun       Date:  2022-10-06       Impact factor: 17.694

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.