RT Journal Article SR Electronic(1) A1 Satoh, Yuto A1 Yonemori, Saeka A1 Hirose, Mitsuhiro A1 Shogaki, Hiroko A1 Wakimoto, Hiroshi A1 Kitagawa, Yoshinori A1 Gotoh, Bin A1 Shirai, Tsuyoshi A1 Takahashi, Ken-ichi A1 Itoh, MasaeYR 2017 T1 A residue located at the junction of the head and stalk regions of measles virus fusion protein regulates membrane fusion by controlling conformational stability JF Journal of General Virology, VO 98 IS 2 SP 143 OP 154 DO https://doi.org/10.1099/jgv.0.000670 PB Microbiology Society, SN 1465-2099, AB The fusion (F) protein of measles virus performs refolding from the thermodynamically metastable prefusion form to the highly stable postfusion form via an activated unstable intermediate stage, to induce membrane fusion. Some amino acids involved in the fusion regulation cluster in the heptad repeat B (HR-B) domain of the stalk region, among which substitution of residue 465 by various amino acids revealed that fusion activity correlates well with its side chain length from the Cα (P<0.01) and van der Waals volume (P<0.001), except for Phe, Tyr, Trp, Pro and His carrying ring structures. Directed towards the head region, longer side chains of the non-ring-type 465 residues penetrate more deeply into the head region and may disturb the hydrophobic interaction between the stalk and head regions and cause destabilization of the molecule by lowering the energy barrier for refolding, which conferred the F protein enhanced fusion activity. Contrarily, the side chain of ring-type 465 residues turned away from the head region, resulting in not only no contact with the head region but also extensive coverage of the HR-B surface, which may prevent the dissociation of the HR-B bundle for initiation of membrane fusion and suppress fusion activity. Located in the HR-B domain just at the junction between the head and stalk regions, amino acid 465 is endowed with a possible ability to either destabilize or stabilize the F protein depending on its molecular volume and the direction of the side chain, regulating fusion activity of measles virus F protein., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000670