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Volume 28, Number 3—March 2022
Research

Novel Hendra Virus Variant Detected by Sentinel Surveillance of Horses in Australia

Edward J. Annand1Comments to Author , Bethany A. Horsburgh1, Kai Xu, Peter A. Reid, Ben Poole, Maximillian C. de Kantzow, Nicole Brown, Alison Tweedie, Michelle Michie, John D. Grewar, Anne E. Jackson, Nagendrakumar B. Singanallur, Karren M. Plain, Karan Kim, Mary Tachedjian, Brenda van der Heide, Sandra Crameri, David T. Williams, Cristy Secombe, Eric D. Laing, Spencer Sterling, Lianying Yan, Louise Jackson, Cheryl Jones, Raina K. Plowright, Alison J. Peel, Andrew C. Breed, Ibrahim Diallo, Navneet K. Dhand, Philip N. Britton, Christopher C. Broder, Ina Smith2, and John-Sebastian Eden2
Author affiliations: EquiEpiVet, Equine Veterinary and One Health Epidemiology, Aireys Inlet, Victoria, Australia (E.J. Annand); Department of Agriculture, Water, and the Environment Epidemiology and One Health Section, Canberra (E.J. Annand, M.C. de Kantzow, A.C. Breed); University of Sydney School of Veterinary Science and Institute for Infectious Diseases, Sydney, New South Wales, Australia (E.J. Annand, N. Brown, A. Tweedie, A.E. Jackson, K.M. Plain, N.K. Dhand); CSIRO Health and Biosecurity Black Mountain Laboratories, Canberra, Australian Capital Territory, Australia (E.J. Annand, M. Michie, I. Smith); Westmead Institute for Medical Research, Sydney (B.A. Horsburgh, K. Kim, J.-S. Eden); University of Sydney School of Medicine, Sydney (B.A. Horsburgh, C. Jones, P.N. Britton, J.-S. Eden); Ohio State University College of Veterinary Medicine, Columbus, Ohio, USA (K. Xu); Private equine veterinary practice, Brisbane, Queensland, Australia (P.A. Reid); Cooroora Veterinary Clinic, Cooroy, Queensland, Australia (B. Poole); JData, Cape Town, South Africa (J.D. Grewar); University of Pretoria, Pretoria, South Africa (J.D. Grewar); CSIRO Australian Centre for Disease Preparedness, Geelong, Victoria, Australia (N.B. Singanallur, M. Tachedjian, B. van der Heide, S. Crameri, D.T. Williams); Murdoch University School of Veterinary Medicine and The Animal Hospital, Murdoch, Western Australia, Australia (C. Secombe); Uniformed Services University of the Health Sciences Microbiology and Immunology, Bethesda, Maryland, USA (E.D. Laing, S. Sterling, L. Yan, C.C. Broder); Queensland Department of Agriculture and Fisheries Biosecurity Sciences Laboratory, Brisbane (L. Jackson, I. Diallo); Children’s Hospital at Westmead, Infectious Diseases, Sydney (C. Jones, P.N. Britton); Montana State University, Bozeman, Montana, USA (R.K. Plowright); Griffith University Centre for Planetary Health and Food Security, Brisbane (A.J. Peel); University of Queensland School of Veterinary Science, Gatton, Queensland, Australia (A.C. Breed)

Main Article

Figure 5

In silico modeling of HeV) from a horse in Australia. A, B) The translated protein sequence encoded by the HeV-var variant G gene was modeled using the known protein structure of the prototype virus bound to the human mAb m102.4 (A) and the receptor ephrinB2 (B). Side views (at left) of the interactions between the HeV G protein and the 2 binding partners highlight key binding residues (as sticks) and the variant positions (orange) relative to the m102.4 (heavy chain in teal and light chain in green) and ephrinB2 (in yellow). Zoomed top views (at right) of the HeV G and m102.4/ephrinB2 binding interface highlight specific interactions by the complementarity-determining regions of the mAb and G-H loop of the receptor ephrinB2. These data show that variable positions do not occur at critical epitopes at the HeV G and m102.4 binding interface and have very minor effect on the receptor ephrinB2 binding. C) Alignment of the prototypic and variant HeV strain G proteins. Variable positions are highlighted in color. F, fusion; G, glycoprotein; HeV, Hendra virus; mAb, monoclonal antibody.

Figure 5. In silico modeling of HeV) from a horse in Australia. A, B) The translated protein sequence encoded by the HeV-var variant G gene was modeled using the known protein structure of the prototype virus bound to the human mAb m102.4 (A) and the receptor ephrinB2 (B). Side views (at left) of the interactions between the HeV G protein and the 2 binding partners highlight key binding residues (as sticks) and the variant positions (orange) relative to the m102.4 (heavy chain in teal and light chain in green) and ephrinB2 (in yellow). Zoomed top views (at right) of the HeV G and m102.4/ephrinB2 binding interface highlight specific interactions by the complementarity-determining regions of the mAb and G-H loop of the receptor ephrinB2. These data show that variable positions do not occur at critical epitopes at the HeV G and m102.4 binding interface and have very minor effect on the receptor ephrinB2 binding. C) Alignment of the prototypic and variant HeV strain G proteins. Variable positions are highlighted in color. F, fusion; G, glycoprotein; HeV, Hendra virus; mAb, monoclonal antibody.

Main Article

1These authors contributed equally to this article.

2These senior authors contributed equally to this article.

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