Structural analysis of human respiratory syncytial virus P protein: identification of intrinsically disordered domains
Braz. j. microbiol
;
42(1): 340-345, Jan.-Mar. 2011. ilus
Article
Dans Anglais
| LILACS
| ID: lil-571408
ABSTRACT
Human Respiratory Syncytial Virus P protein plus the viral RNA, N and L viral proteins, constitute the viral replication complex. In this report we describe that HRSV P protein has putative intrinsically disordered domains predicted by in silico methods. These two domains, located at the amino and caboxi terminus, were identified by mass spectrometry analysis of peptides obtained from degradation fragments observed in purified P protein expressed in bacteria. The degradation is not occurring at the central oligomerization domain, since we also demonstrate that the purified fragments are able to oligomerize, similarly to the protein expressed in cells infected by HRSV. Disordered domains can play a role in protein interaction, and the present data contribute to the comprehension of HRSV P protein interactions in the viral replication complex.
Texte intégral:
Disponible
Indice:
LILAS (Amériques)
Sujet Principal:
Fragments peptidiques
/
Spectrométrie de masse
/
Réplication virale
/
Techniques in vitro
/
ARN viral
/
Chromatographie en phase liquide
/
Virus respiratoire syncytial humain
Type d'étude:
Etude diagnostique
Limites du sujet:
Humains
langue:
Anglais
Texte intégral:
Braz. j. microbiol
Thème du journal:
Microbiologie
Année:
2011
Type:
Article
/
descriptif de projet
Pays d'affiliation:
Brésil
/
États-Unis d'Amérique
Institution/Pays d'affiliation:
Harvard Institutes of Medicine/US
/
Universidade de São Paulo/BR
Documents relatifs à ce sujet
MEDLINE
...
LILACS
LIS