9SCW

Crystal structure of Coxsackie B1 virus-like particle delta-palxa

This is a non-PDB format compatible entry.

Summary for 9SCW

• Entry DOI: 10.2210/pdb9scw/pdb
• Descriptor: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (5 entities in total)
• Functional Keywords: coxsackievirus b1, virus-like particle, virus like particle
• Biological source: Coxsackievirus B1; More
• Total number of polymer chains: 70
• Total formula weight: 1778617.11

Authors

Haikarainen, T. (deposition date: 2025-08-12, release date: 2025-10-08)

Primary citation

Soppela, S.,Gonzalez-Rodriguez, M.,Stone, V.M.,Mustonen, I.,Jouppila, N.V.V.,Lampinen, V.,Haikarainen, T.,Flodstrom-Tullberg, M.,Junttila, I.S.,Hankaniemi, M.M.
Coxsackie B1 virus-like particle vaccine modified to exclude a highly conserved immunoreactive region from the capsid induces potent neutralizing antibodies and protects against infection in mice.
J.Biomed.Sci., 32:86-86, 2025

PubMed Abstract: Enteroviruses, including Coxsackie B (CVB) viruses, can cause severe diseases such as myocarditis, pancreatitis, and meningitis. Vaccines can prevent these complications, but conserved non-neutralizing epitopes in the viral capsid may limit their effectiveness. The immunodominant PALXAXETG motif, located in the VP1 N-terminus, is a highly conserved region in enteroviruses that elicits non-neutralizing antibody responses. Virus-like particles (VLPs) offer a safe and effective vaccine platform because of their structural similarity to native viruses but lack viral genetic material. Importantly, VLPs can be structurally modified to exclude specific epitopes.

PubMed: 40922007
DOI: 10.1186/s12929-025-01183-1

Experimental method

X-RAY DIFFRACTION (3.2 Å)