Decoding tick receptor mechanisms in Kyasanur forest disease virus transmission: structural insights into vector competence
- 1ICAR-National Institute of Veterinary Epidemiology and Disease Informatics, Ramagondanahalli, Yelahanka New Town, Bengaluru, Karnataka India
Abstract
Kyasanur forest disease virus (KFDV), a tick-borne flavivirus of major zoonotic concern, is responsible for recurrent outbreaks in Southern India. Although various tick species have been implicated in KFDV transmission, the molecular determinants of viral entry and vector competence remain undefined. To investigate this, we employed in silico structural approaches integrating cross-species receptor mining, protein–protein docking, and molecular dynamics simulations. This analysis revealed conserved homologues of mammalian flavivirus and arthropod receptors across Ixodid ticks with Dermacentor and Rhipicephalus spp. having the highest receptor repertoire. Docking analyses with the KFDV envelope protein demonstrated strong interactions with heat shock protein 70 (HSP70) and C-type lectins (CTLs) from Dermacentor silvarum followed by Ornithodorus turicata and Rhipicephalus microplus. Furthermore, envelope dimerization enhanced binding with selected receptors, and simulations confirmed a stable, high-affinity envelope–D. silvarum CTL complex (ΔG = − 45.24 ± 1.28 kcal/mol), stabilized by extensive hydrogen bond networks centred on domain III residues. The observed variation in EDIII-mediated receptor binding suggests that differential structural compatibility may influence host receptor recognition and early stages of virus–vector interaction across tick species. Together, these findings provide preliminary structural insights into KFDV–tick receptor interactions and lay the molecular groundwork for understanding species-specific determinants of vector competence.
Supplementary Information: The online version contains supplementary material available at https://doi.org/10.1186/s12866-026-05414-9.
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BibTeX
@article{pooja2026decoding,
title = {{Decoding tick receptor mechanisms in Kyasanur forest disease virus transmission: structural insights into vector competence}},
author = {Pillenahalli Sadashivappa Pooja and Anand Shirisha and Venugopal Nandish and Suresh Bindu and Mandrira Ramakrishna Namrutha and Sahal Paladan and Bhimanagoud Kumbar and Sathish Bhadravati Shivachandra and Mohammed Mudassar Chanda},
journal = {BMC Microbiology},
year = {2026},
month = aug,
doi = {10.1186/s12866-026-05414-9},
url = {https://doi.org/10.1186/s12866-026-05414-9},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - Decoding tick receptor mechanisms in Kyasanur forest disease virus transmission: structural insights into vector competence
AU - Pillenahalli Sadashivappa Pooja
AU - Anand Shirisha
AU - Venugopal Nandish
AU - Suresh Bindu
AU - Mandrira Ramakrishna Namrutha
AU - Sahal Paladan
AU - Bhimanagoud Kumbar
AU - Sathish Bhadravati Shivachandra
AU - Mohammed Mudassar Chanda
PY - 2026
DA - 2026/08/06
JO - BMC Microbiology
DO - 10.1186/s12866-026-05414-9
UR - https://doi.org/10.1186/s12866-026-05414-9
AB - Kyasanur forest disease virus (KFDV), a tick-borne flavivirus of major zoonotic concern, is responsible for recurrent outbreaks in Southern India. Although various tick species have been implicated in KFDV transmission, the molecular determinants of viral entry and vector competence remain undefined. To investigate this, we employed in silico structural approaches integrating cross-species receptor mining, protein–protein docking, and molecular dynamics simulations. This analysis revealed conserved homologues of mammalian flavivirus and arthropod receptors across Ixodid ticks with Dermacentor and Rhipicephalus spp. having the highest receptor repertoire. Docking analyses with the KFDV envelope protein demonstrated strong interactions with heat shock protein 70 (HSP70) and C-type lectins (CTLs) from Dermacentor silvarum followed by Ornithodorus turicata and Rhipicephalus microplus. Furthermore, envelope dimerization enhanced binding with selected receptors, and simulations confirmed a stable, high-affinity envelope–D. silvarum CTL complex (ΔG = − 45.24 ± 1.28 kcal/mol), stabilized by extensive hydrogen bond networks centred on domain III residues. The observed variation in EDIII-mediated receptor binding suggests that differential structural compatibility may influence host receptor recognition and early stages of virus–vector interaction across tick species. Together, these findings provide preliminary structural insights into KFDV–tick receptor interactions and lay the molecular groundwork for understanding species-specific determinants of vector competence. Supplementary Information: The online version contains supplementary material available at https://doi.org/10.1186/s12866-026-05414-9.
SN - 1471-2180
ER -