The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Putative staphylococcal enterotoxin possesses two common structural motifs for MHC-II binding
Open accessPublished version of a preprint
Abstract
Staphylococcus aureus has become a significant cause of health risks in humankind. Staphylococcal superantigens (SAgs) or enterotoxins are the key virulent factors that can exhibit acute diseases to severe life-threatening conditions. Recent literature reports S. aureus has steadily gained new enterotoxin genes over the past few decades. In spite of current knowledge of the established SAgs, several questions on putative enterotoxins are still remaining unanswered. Keeping that in mind, this study sheds light on a putative enterotoxin SEl26 to characterize its structural and functional properties. In-silico analyses indicate its close relation with the conventional SAgs, especially the zinc-binding SAgs. Additionally, important residues that are vital for the T-cell receptor (TcR) and major histocompatibility complex class II (MHC-II) interaction were predicted and compared with established SAgs. Besides, our biochemical analyses exhibited the binding of this putative enterotoxin with MHC-II, followed by regulating pro-inflammatory and anti-inflammatory cytokines.
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Metadata
- Authors
- Rahman, S., Saha, S., Dasgupta, S. B., & Das, A. K.
- Affiliations
- Indian Institute of Technology Kharagpur (IN)
- Corresponding author
- Das, Amit Kumar
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2024-01
- Volume
- 256
- Issue
- Pt 1
- Pages
- 128437
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W4388997196
- Cited by
- 0
- References
- 43
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- International Journal of Biological Macromolecules (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Funders
- Science and Engineering Research Board (CRG/2020/002622, EMR/2016/002825)
- Indian Institute of Technology Kharagpur
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- staphylococcal enterotoxins, staphylococcal superantigens, MHC class II binding, T cell receptor interaction, cytokine regulation, inflammatory cytokines, anti-inflammatory cytokines, protein structural motifs
- MeSH terms
- Amino Acid Sequence, Histocompatibility Antigens Class II, Binding Sites, Enterotoxins, Staphylococcus, Staphylococcus aureus, Superantigens
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- Rahman, S., Saha, S., Dasgupta, S. B., & Das, A. K. (2024). Putative staphylococcal enterotoxin possesses two common structural motifs for MHC-II binding. International Journal of Biological Macromolecules. https://doi.org/10.1016/j.ijbiomac.2023.128437
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
