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| Fang,Longfa; Wang,Bo; Zhou,Zishan; Yang,Sujuan; Shu,Changlong; Song,Fuping; Bravo,Alejandra; Soberón,Mario; Zhang,Jie. |
| Background: Bacillus thuringiensis Cry toxins bind with different insect midgut proteins leading to toxin oligomerization, membrane insertion and pore formation. However, different Cry toxins had been shown to readily form high molecular weight oligomers or aggregates in solution in the absence of receptor interaction. The role of Cry oligomers formed in solution remains uncertain. The Cry9A proteins show high toxicity against different Lepidoptera, and no-cross resistance with Cry1A. Results: Cry9Aa655 protein formed oligomers easily in solution mediated by disulfide bonds, according to SDS-PAGE analysis under non-reducing and reducing conditions. However, oligomerization is not observed if Cry9Aa655 is activated with trypsin, suggesting that cysteine... |
| Tipo: Journal article |
Palavras-chave: Cry9Aa655; Disulfide bonds; Oligomerization; Insecticidal activity. |
| Ano: 2016 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300006 |
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| Simabuco,Fernando M; Asara,John M; Guerrero,Manuel C; Libermann,Towia A; Zerbini,Luiz F; Ventura,Armando M. |
| 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... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Human respiratory syncytial virus; P protein; Intrinsically disordered domains; Oligomerization. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000100043 |
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