FIG 5.

Conservation of L and P proteins. (A to C) P and L proteins from members of the Vesiculovirus and Sprivivirus genera were aligned in Clustal (37). (A) P proteins were aligned against VSV P 76 to 106. The most strongly interacting fragment, P 97 to 106, is highlighted with a red bar. (B and C) L proteins were aligned against VSV L 1414 to 1436 (B) and 1529 to 1547 (C), the two fragments implicated by HDX-MS. (D to F) L proteins from members of Mononegavirales were aligned in Clustal and subjected to secondary structure prediction. (D and E) L proteins were aligned against VSV L 1414 to 1436 (D) and 1529 to 1547 (E). (F) Secondary structure prediction was carried out for each putative connector sequence using PSIPRED (38). The predicted helical content (Hel_pred) is listed for each protein, except for VSV L, in which the authentic helical content is provided from the existing structure (PDB ID 5A22). VSIV, Indiana vesicular stomatitis virus; VSNV, New Jersey vesicular stomatitis virus; VSAV, Alagoas vesicular stomatitis virus; CARV, Carajas virus; CHPV, Chandipura virus; COCV, Cocal virus; ISFV, Isfahan virus; MARAV, Maraba virus; PIRYV, Piry virus; JURV, Jurona virus; PERIV, Perinet virus; YUBOV, Yug Bogdanovac virus; PFRV, pike fry virus; SVCV, spring viremia of carp virus; hRSV, human respiratory syncytial virus; hMPV, human metapneumovirus; ZEBV, Ebola virus; MARV, Marburg virus; PIV3, parainfluenza virus type 3; SeV, Sendai virus; HENV, Hendra virus; NIPV, Nipah virus; SV5, simian virus 5; MuV, mumps virus; MeV, measles virus; NDV, Newcastle disease virus. Absolute (*), strong (:), and weak (.) conservation is denoted above the alignments.