Functional Analysis of Individual Oligosaccharide Chains of Sendai Virus Hemagglutinin-neuraminidase Protein

Segawa, Hiroaki; Inakawa, Akira; Yamashita, Tetsuro; Taira, Hideharu

doi:10.1271/bbb.67.592

Cited by 12 publications

(3 citation statements)

References 30 publications

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“…Furthermore, we note that the observed mode of MosV-RBPb and NarV-RBPb dimerization is in agreement with the location of N-linked glycosylation sequons (NXS/T where X≠P). Indeed, although MosV-RBPb and NarV-RBPb lack the high level of glycosylation inherent to most paramyxoviral proteins [42,[44][45][46][47][48][49][50], in line with the hypothesis that glycosylation is not expected to be occluded within protein-protein interfaces, the single N-linked sites observed in the bpropeller domain of both MosV-RBP (Asn319) and NarV-RBP (Asn575) are directed away from and do not interfere with the observed RBP homodimers. Furthermore, we note that the MosV/NarV exhibit the greatest level of structural conservation in the region of this oligomeric interface with respect to the rest of the molecule (Fig.…”

Section: Narmoviral Rbps Are Dimeric In Solution and In The Crystal S...mentioning

confidence: 61%

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein

Stelfox

Oguntuyo

Rissanen

et al. 2022

Preprint

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Increased viral surveillance has led to the isolation and identification of numerous uncharacterized paramyxoviruses, rapidly expanding our understanding of paramyxoviral diversity beyond the bounds of known genera. Despite this diversity, a key feature that unites paramyxoviruses is the presence of a receptor-binding protein, RBP, which facilitates host-cell attachment and plays a fundamental role in determining host-range. Here, we study the RBP presented on the surface of rodent-borne paramyxoviruses Mossman and Nariva (MosV and NarV, respectively), viruses that constitute founding members of the recently definedNarmovirusgenus within theParamyxoviridaefamily. Crystallographic analysis of the C-terminal head region of the dimeric MosV and NarV RBPs demonstrates that while these glycoproteins retain the canonical six-bladed β-propeller fold found in other paramyxoviral RBPs, they lack the structural motifs associated with established paramyxovirus host-cell receptor entry pathways. Consistent with MosV-RBP and NarV-RBP undergoing a distinct entry pathway from other characterized paramyxoviruses, structure-based phylogenetic analysis demonstrates that these six-bladed β-propeller head domains form a singular structural class that is distinct from other paramyxoviral RBPs. Additionally, using an integrated crystallographic and small angle X-ray scattering analysis, we confirm that MosV-RBP and NarV-RBP form homodimeric arrangements that are distinct from those adopted by other paramyxovirus RBPs. Altogether, this investigation provides a molecular-level blueprint of the narmovirus RBP that broadens our understanding of the structural space and functional diversity available to paramyxovirus RBPs.

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Section: Narmoviral Rbps Are Dimeric In Solution and In The Crystal S...mentioning

confidence: 61%

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein

Stelfox

Oguntuyo

Rissanen

et al. 2022

Preprint

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show abstract

“…Beyond the ER, both NG and DBs can be further edited. For example, after exiting the ER, N -glycans can be processed in the Golgi [ 21 ]. For DBs, a number of enzymes both inside and outside of cells can break and reform these covalent bonds, which often function as switches to activate or suppress host protein functions [ 22 ].…”

Section: Molecular Foundationsmentioning

confidence: 99%

Hidden Relationships between N-Glycosylation and Disulfide Bonds in Individual Proteins

Bakshi

Pham

Kaur

et al. 2022

IJMS

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N-Glycosylation (NG) and disulfide bonds (DBs) are two prevalent co/post-translational modifications (PTMs) that are often conserved and coexist in membrane and secreted proteins involved in a large number of diseases. Both in the past and in recent times, the enzymes and chaperones regulating these PTMs have been constantly discovered to directly interact with each other or colocalize in the ER. However, beyond a few model proteins, how such cooperation affects N-glycan modification and disulfide bonding at selective sites in individual proteins is largely unknown. Here, we reviewed the literature to discover the current status in understanding the relationships between NG and DBs in individual proteins. Our results showed that more than 2700 human proteins carry both PTMs, and fewer than 2% of them have been investigated in the associations between NG and DBs. We summarized both these proteins with the reported relationships in the two PTMs and the tools used to discover the relationships. We hope that, by exposing this largely understudied field, more investigations can be encouraged to unveil the hidden relationships of NG and DBs in the majority of membranes and secreted proteins for pathophysiological understanding and biotherapeutic development.

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“…Similar to HPIV-3, SeV HN utilizes three of its four potential N -glycosylation sites, and 9% of its mass can be attributed to glycan modifications ( Kohama et al 1978 ; Segawa et al 2003 ). These N -glycans play a significant role in intracellular transport and fusion ( Segawa et al 2003 ). Fifteen percent of the mass of SeV F is attributable to O -glycan modifications ( Kohama et al 1978 ), and SeV F has three N -glycosylation sites.…”

Section: Introductionmentioning

confidence: 99%

Addicted to sugar: roles of glycans in the orderMononegavirales

et al. 2018

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Glycosylation is a biologically important protein modification process by which a carbohydrate chain is enzymatically added to a protein at a specific amino acid residue. This process plays roles in many cellular functions, including intracellular trafficking, cell-cell signaling, protein folding, and receptor binding. While glycosylation is a common host cell process, it is utilized by many pathogens as well. Protein glycosylation is widely employed by viruses for both host invasion and evasion of host immune responses. Thus better understanding of viral glycosylation functions has potential applications for improved antiviral therapeutic and vaccine development. Here, we summarize our current knowledge on the broad biological functions of glycans for the Mononegavirales, an order of enveloped negative-sense single-stranded RNA viruses of high medical importance that includes Ebola, Rabies, Measles, and Nipah viruses. We discuss glycobiological findings by genera in alphabetical order within each of eight Mononegavirales families, namely the bornaviruses, filoviruses, mymonaviruses, nyamiviruses, paramyxoviruses, pneumoviruses, rhabdoviruses, and sunviruses.

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Functional Analysis of Individual Oligosaccharide Chains of Sendai Virus Hemagglutinin-neuraminidase Protein

Cited by 12 publications

References 30 publications

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein

Hidden Relationships between N-Glycosylation and Disulfide Bonds in Individual Proteins

Addicted to sugar: roles of glycans in the orderMononegavirales

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