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The **Newcastle disease virus fusion protein (NDV F protein)** is a class I viral membrane fusion glycoprotein located on the surface of the Newcastle disease virus (NDV), an avian paramyxovirus. Synthesized as a precursor (F0), it is cleaved by host proteases into two disulfide-linked subunits (F1 and F2); this cleavage is essential for the infectious and fusogenic properties of the virus[1][2][8]. The fusion protein enables viral entry by promoting the merging of the viral envelope with the host cell membrane, thereby allowing the viral genome to enter the host cell[3][4][6]. The sequence at the cleavage site is a primary determinant of tissue tropism and virulence: a multibasic cleavage site is associated with systemic, highly virulent infection, while a monobasic site restricts infection to the respiratory and digestive tracts[1][6][8]. The F protein is also the main target for neutralizing antibodies, making it a key antigen in vaccine design and immunodiagnostics[7]. Point mutations, antigenic drift, or recombination in F protein's antigenic regions can influence vaccine efficacy and facilitate outbreak persistence[7]. The structure of the F protein undergoes a dramatic conformational change during membrane fusion, forming a six-helix bundle in its post-fusion state[3][4].\n\nThe NDV F protein is a validated therapeutic and vaccine target for both disease prevention and potential oncolytic virotherapy due to its immunogenic and fusogenic properties[2]. There are no approved direct-acting drugs, but experimental inhibitors and neutralizing antibodies are studied. The protein is part of the larger class of viral envelope fusion proteins found in other paramyxoviruses such as parainfluenza and measles viruses[8].
Inhibition of membrane fusion (by antibodies or peptide inhibitors)[7] Neutralization of viral infectivity (by antibodies)[7]
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