IRIS – Institutional Research Information System
IRIS è il sistema di gestione della ricerca dell’Università degli Studi di Milano-Bicocca.Il repository BOA è il modulo del sistema dedicato alla raccolta e alla disseminazione della produzione scientifica di Ateneo. Le pubblicazioni sono ricercabili per parola chiave attraverso il box nella barra orizzontale in alto oppure, mediante il pulsante Sfoglia, per "Afferenza", "Autore", "Titolo", "Tipologia" o "Settore scientifico-disciplinare".
IRIS contiene inoltre alcuni moduli dedicati alla registrazione dei progetti e dei contratti, e alla reportistica avanzata per le attività di valutazione della ricerca
EnglishRIG-I-like receptors (RLRs) are nucleic acid sensors that activate antiviral innate immune response. These molecules recognize diverse non-self RNA substrates and are antagonized by several viral inhibitors. We performed an evolutionary analysis of RLR genes (RIG-I, MDA5, and LGP2) in mammals. Results indicated that purifying selection had a dominant role in driving the evolution of RLRs. However, application of maximum-likelihood analyses identified several positions that evolved adaptively. Positively selected sites are located in all domains of MDA5 and RIG-I, whereas in LGP2 they are confined to the helicase domain. In both MDA5 and RIG-I, the linkers separating the caspase activation and recruitment domain and the helicase domain represented preferential targets of positive selection. Independent selective events in RIG-I and LGP2 targeted the corresponding site (Asp421 and Asp179, respectively) within a protruding α-helix that grips the V-shaped structure formed by the pincer. Most of the positively selected sites in MDA5 are in regions unique to this RLR, including a characteristic insertion within the helicase domain. Additional selected sites are located at the contact interface between MDA5 monomers, in spatial proximity to a positively selected human polymorphism (Arg843His) and immediately external to the parainfluenza virus 5 V protein binding region. Structural analyses suggested that the positively selected His834 residue is involved in parainfluenza virus 5 V protein binding. Data herein suggest that RLRs have been engaged in host-virus genetic conflict leading to diversifying selection and indicate parallel evolution at the same site in RIG-I and LGP2, a position likely to be of central importance in antiviral responses. © 2013 Elsevier Ltd.
Cagliani, R., Forni, D., Tresoldi, C., Pozzoli, U., Filippi, G., Rainone, V., et al. (2014). RIG-I-like receptors evolved adaptively in mammals, with parallel evolution at LGP2 and RIG-I. JOURNAL OF MOLECULAR BIOLOGY, 426(6), 1351-1365.
| Citazione: | Cagliani, R., Forni, D., Tresoldi, C., Pozzoli, U., Filippi, G., Rainone, V., et al. (2014). RIG-I-like receptors evolved adaptively in mammals, with parallel evolution at LGP2 and RIG-I. JOURNAL OF MOLECULAR BIOLOGY, 426(6), 1351-1365. | |
| Tipo: | Articolo in rivista - Articolo scientifico | |
| Carattere della pubblicazione: | Scientifica | |
| Presenza di un coautore afferente ad Istituzioni straniere: | No | |
| Titolo: | RIG-I-like receptors evolved adaptively in mammals, with parallel evolution at LGP2 and RIG-I | |
| Autori: | Cagliani, R; Forni, D; Tresoldi, C; Pozzoli, U; Filippi, G; Rainone, V; De Gioia, L; Clerici, M; Sironi, M | |
| Autori: | ||
| Data di pubblicazione: | 2014 | |
| Lingua: | English | |
| Rivista: | JOURNAL OF MOLECULAR BIOLOGY | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/j.jmb.2013.10.040 | |
| Appare nelle tipologie: | 01 - Articolo su rivista |
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