9TKM

CryoEM structure of coxsackievirus B1 virus-like particle with VP4 deletion

Summary for 9TKM

Entry DOI	10.2210/pdb9tkm/pdb
EMDB information	56033
Descriptor	Capsid protein VP1, Capsid protein VP2, Capsid protein VP3 (3 entities in total)
Functional Keywords	cvb1, vlp, vaccine candidate, enterovirus, virus like particle
Biological source	Coxsackievirus B1 More
Total number of polymer chains	3
Total formula weight	86603.60
Authors	Levanova, A.L.,Guryanov, S.,Ahmad, K.L.L.,Butcher, S.J. (deposition date: 2025-12-10, release date: 2026-04-08)
Primary citation	Soppela, S.,Kyrolainen, H.M.,Levanova, A.,Nekoua, M.P.,Gonzalez-Rodriguez, M.,Lehto, H.,Ahmad, K.L.L.,Guryanov, S.,Hytonen, V.P.,Laitinen, O.H.,Junttila, I.S.,Hober, D.,Butcher, S.J.,Hankaniemi, M.M. Coxsackie B1 virus-like particle that lacks VP4 protein demonstrates improved vaccine scalability, stability and immunogenicity. J.Biomed.Sci., 33:-, 2026 Cited by PubMed Abstract: Enteroviruses, including coxsackievirus B1 (CVB1), cause severe diseases such as myocarditis and meningitis, but vaccines are lacking for most enteroviruses. Conserved and immunodominant epitopes, such as VP4 region and VP1 N-terminus may limit vaccine efficacy by inducing non-neutralizing antibody responses. Virus-like particles (VLPs) mimic native viruses without genetic material and can be engineered to exclude epitopes. To address these challenges, we developed a CVB1-VLP lacking VP4. PubMed: 41888844 DOI: 10.1186/s12929-026-01229-y PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (2.7 Å)

Structure validation