Lamb RA, Parks GD (2007) Paramyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM, editors. Fields Virology: Lippincott, Williams and Wilkins. pp. 1449–1496.
[2]
Eaton BT, Broder CC, Middleton D, Wang LF (2006) Hendra and Nipah viruses: different and dangerous. Nat Rev Microbiol 4: 23–35.
[3]
Eaton BT, Mackenzie JS, Wang L-F (2007) Henipaviruses. In: Knipe DM, Howley PM, editors. Fields Virology: Lippincott, Williams and Wilkins. pp. 1587–1600.
[4]
van den Hoogen BG, de Jong JC, Groen J, Kuiken T, de Groot R, et al. (2001) A newly discovered human pneumovirus isolated from young children with respiratory tract disease. Nat Med 7: 719–724.
[5]
Collins PL, Crowe JE (2007) Respiratory syncytial virus and metapneumovirus. In: Knipe DM, Howley PM, editors. Fields Virology: Lippincott, Williams and Wilkins. pp. 1601–1646.
[6]
Smith EC, Popa A, Chang A, Masante C, Dutch RE (2009) Viral entry mechanisms: the increasing diversity of paramyxovirus entry. FEBS J.
[7]
Aguilar HC, Ataman ZA, Aspericueta V, Fang AQ, Stroud M, et al. (2009) A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F). J Biol Chem 284: 1628–1635.
[8]
Bonaparte MI, Dimitrov AS, Bossart KN, Crameri G, Mungall BA, et al. (2005) Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus. Proc Natl Acad Sci U S A 102: 10652–10657.
[9]
Negrete OA, Levroney EL, Aguilar HC, Bertolotti-Ciarlet A, Nazarian R, et al. (2005) EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436: 401–405.
[10]
Xu K, Rajashankar KR, Chan YP, Himanen JP, Broder CC, et al. (2008) Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci U S A 105: 9953–9958.
[11]
Bossart KN, Tachedjian M, McEachern JA, Crameri G, Zhu Z, et al. (2008) Functional studies of host-specific ephrin-B ligands as Henipavirus receptors. Virology 372: 357–371.
[12]
Pager CT, Dutch RE (2005) Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J Virol 79: 12714–12720.
[13]
Meulendyke KA, Wurth MA, McCann RO, Dutch RE (2005) Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein. J Virol 79: 12643–12649.
[14]
Diederich S, Moll M, Klenk HD, Maisner A (2005) The nipah virus fusion protein is cleaved within the endosomal compartment. J Biol Chem 280: 29899–29903.
[15]
Whitman SD, Smith EC, Dutch RE (2009) Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation. J Virol 83: 8998–9001.
[16]
Biacchesi S, Pham QN, Skiadopoulos MH, Murphy BR, Collins PL, et al. (2005) Infection of nonhuman primates with recombinant human metapneumovirus lacking the SH, G, or M2-2 protein categorizes each as a nonessential accessory protein and identifies vaccine candidates. J Virol 79: 12608–12613.
[17]
Schowalter RM, Smith SE, Dutch RE (2006) Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low pH. J Virol 80: 10931–10941.
[18]
Herfst S, Mas V, Ver LS, Wierda RJ, Osterhaus AD, et al. (2008) Low pH induced membrane fusion mediated by human metapneumoviruses F protein is a rare, strain dependent phenomenon. J Virol 82: 8891–8895.
[19]
Schowalter RM, Chang A, Robach JG, Buchholz UJ, Dutch RE (2009) Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry. J Virol 83: 1511–1522.
[20]
Kolokoltsov AA, Deniger D, Fleming EH, Roberts NJ Jr, Karpilow JM, et al. (2007) Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus. J Virol 81: 7786–7800.
