Work

The solution supramolecular structure of α2 → 8 polysialic acid suggests a structural cause for its low immunogenicity

Year: 2025

Type: article

Abstract: α2 → 8 polysialic acid (polySia), the capsular polysaccharide on Neisseria meningitidis serogroup B and Escherichia coli K1, elicits poor immunogenic properties. A solution structure might clarify the cause. From X-ray and neutron small-angle scattering, we find that the solution supramolecular structure of polySia exhibits parallel-chain binding. Also, striking structural changes occur upon the addition of calcium to these solutions but still with the parallel motif. The major histocompatibility complex requires entities in the molecular weight range of 600-3000 Da, but the solution structures determined here argue that in endosomes polySia oligomers of the correct size to be immunologically effective are instead bound up as parallel chains. This is expected to reduce the possible concentrations of the effective oligomers and so reduce the immunogenic capability of α2 → 8 polysialic acid.

Source: FEBS Letters

DOI: 10.1002/1873-3468.70032

Author: Kenneth A. Rubinson

Institutions: National Institute of Standards and Technology, Wright State University, NIST Center for Neutron Research

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,980