Wolters kluwer health lippincott williams wilkins powerpoints: The Postfusion Structure of the Heartland Virus Gc Glycoprotein Supports Taxonomic Separation of the Bunyaviral …

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Domain III orientation is bunyavirus family specific. Structural superimposition of each Gc from two members of phenuivirus and hantavirus indicated that Gc proteins in the same genus display similar folds, with root mean square deviations (RMSDs) of 1.010 Å and 1.073 Å, respectively ( Fig. 2A and B ). In contrast, the HRTV and HTNV Gc display different conformations, with an RMSD of 4.600 Å. Using domain I as a reference, the domain III orientation between these two viruses presents in opposite directions ( Fig. 2C ). Moreover, the orientation of domain I dramatically changes from the prefusion to postfusion conformation in phenuiviruses, while domain I displays a similar conformation among hantaviruses. The translocation of domain III from the prefusion to postfusion state between these two genera is different as well. Domain III in phenuivirus and hantavirus pivots 75.1° and 132.6°, respectively. In contrast, the hinge of domain II at the domain I/II junction between these two genera is almost the same, displaying 25.9° and 26° shifts, respectively ( Fig. 2D and E ). Topology diagrams indicate that the two phenuiviruses (SFTSV and HRTV) display similar patterns, with only one 3 10 helix (η2) difference in domain II (see Fig. S1 in the supplemental material). In contrast, the two hantaviruses (PUUV and HTNV) show more secondary structure element diversity in domains II and III (Fig. S2). Specifically, the PUUV Gc has an extra 3 10 helix (η2) and a short β-strand (h) in domain II compared to the contents of HTNV Gc. Additionally, there is an α-helix between β-strands j and k in the PUUV Gc domain II, while HTNV has a 3 10 helix (η2) and a short β-strand (k) instead. In domain III, the HTNV Gc has one β-strand (G) more than the PUUV Gc at its C terminus.

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