Abstract
The recognition of sialic acids by two strains of minute virus of mice (MVM), MVMp (prototype) and MVMi (immunosuppressive), is an essential requirement for successful infection. To understand the potential for recognition of different modifications of sialic acid by MVM, three types of capsids, virus-like particles, wild type empty (no DNA) capsids, and DNA packaged virions, were screened on a sialylated glycan microarray (SGM). Both viruses demonstrated a preference for binding to 9-O-methylated sialic acid derivatives, while MVMp showed additional binding to 9-O-acetylated and 9-O-lactoylated sialic acid derivatives, indicating recognition differences. The glycans recognized contained a type-2 Galβ1-4GlcNAc motif (Neu5Acα2-3Galβ1-4GlcNAc or 3′SIA-LN) and were biantennary complex-type N-glycans with the exception of one. To correlate the recognition of the 3′SIA-LN glycan motif as well as the biantennary structures to their natural expression in cell lines permissive for MVMp, MVMi, or both strains, the N- and O-glycans, and polar glycolipids present in three cell lines used for in vitro studies, A9 fibroblasts, EL4 T lymphocytes, and the SV40 transformed NB324K cells, were analyzed by MALDI-TOF/TOF mass spectrometry. The cells showed an abundance of the sialylated glycan motifs recognized by the viruses in the SGM and previous glycan microarrays supporting their role in cellular recognition by MVM. Significantly, the NB324K showed fucosylation at the non-reducing end of their biantennary glycans, suggesting that recognition of these cells is possibly mediated by the Lewis X motif as in 3′SIA-LeX identified in a previous glycan microarray screen.
Highlights
Viruses serve as robust genome delivery vehicles evolved to utilize an array of intricate strategies for successful infection of target host organisms
MVMp and MVMi showed a preference for binding to sialic acid (SIA) that was methylated at C-9 and not C-8
minute virus of mice (MVM) Binds to Diverse Sialylated Derivatives Glycan arrays attempt to mimic the diversity of glycans present on cell surfaces, and if a virus recognizes a particular type of glycan on these arrays, it suggests that the virus may recognize similar glycans in its natural host
Summary
Viruses serve as robust genome delivery vehicles evolved to utilize an array of intricate strategies for successful infection of target host organisms. Carbohydrates, and lipids constitute receptors for many enveloped and non-enveloped viruses. Glycans (complex carbohydrates) are the major constituents of the cell surface and may be conjugated to proteins or membrane lipid head groups to form glycoproteins and glycolipids, respectively, or are present as glycosaminoglycan (GAG) chains attached within proteoglycans. For most viruses that utilize glycan receptors, the binding is mediated by electrostatic interaction between the viral attachment protein and negatively charged sialic acid (SIA)-containing glycan determinants or sulfated portions of glycosaminoglycans. The virus recognition motif can be spike glycoproteins displayed on the lipid bilayer of enveloped viruses, or specific features, such as protrusions or depressions, conformed on the assembled capsid surface of non-enveloped viruses. The diverse interactions that occur between the viral pathogen and host, especially the recognition of cell surface receptors determines host specificity and tissue tropism. The pathway of entry into the cell and subsequent interactions influence the pathogenic outcome of infection
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