Structure, Immunogenicity and Clinical Value of Chlamydiaphage Capsid Protein 3 / 病毒学报
Chinese Journal of Virology
;
(6): 420-424, 2015.
Artigo
em Chinês
| WPRIM
| ID: wpr-296268
ABSTRACT
We wished to assess the role of chlamydia micro virus capsid protein Vp3 in recombinant molecules, chart its molecular evolution, screen the wild-type strain, and reveal its value in clinical research. Using a protein BLAST multiple-alignment program, we compared various strains of Chlamydia micro virus capsid protein Vp3 sequences. Using a "distance tree" of those results, we created a phylogenetic tree. We applied the Karplus-Schulz method of flexible-region analyses for highly conserved alignments of amino-acid sequences. Gamier-Robson and Chou-Fasman methods were employed to analyze two-level structures of sequences. The Emini method was used for analyses of the accessibility of surface epitopes. Studies of hydrophilic proteins were undertaken using Kyte-Doolittle and Hopp-Woods methods. Analyses of antigen epitopes helped to reveal the antigen index using the Jameson-Wolf method. All sequences in the six strains of chlamydia micro virus capsid protein Vp3 were highly conserved, with the main differences being between Vp3 protein in Chp1 and the other five strains of the micro virus. The viral strain of Vp3 protein was based mainly on micro-alpha helix structures, and multiple epitopes were noted in highly conserved regions. Vp3 protein was highly conserved structurally, and was an important protein of the chlamydiaphage capsid. Vp3 protein has a complicated molecular structure, highly conserved regions with strong immunogenicity, and has considerable research value.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Recombinação Genética
/
Dados de Sequência Molecular
/
Química
/
Chlamydia
/
Sequência de Aminoácidos
/
Sequência Conservada
/
Mapeamento de Epitopos
/
Evolução Molecular
/
Proteínas do Capsídeo
/
Alergia e Imunologia
Idioma:
Chinês
Revista:
Chinese Journal of Virology
Ano de publicação:
2015
Tipo de documento:
Artigo
Similares
MEDLINE
...
LILACS
LIS