Author

O. L. Welsh

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Organism:mouse· 2 Organism:human· 1 Research Focus:variant calling· 1

Frequent Co-Authors

D. M. Sutherland· 3 shared T. S. Dermody· 3 shared A. J. Lentscher· 1 shared B. Prasad· 1 shared C. Guzman-Cardozo· 1 shared D. Alsteens· 1 shared G. M. Taylor· 1 shared J. J. Knowlton· 1 shared

Activity by Year

2021-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersMicrobiology

D. M. Sutherland

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Chikungunya virus vaccine candidate incorporating synergistic mutations is attenuated and protects against virulent virus challenge

A. J. Lentscher, N. McAllister, K. A. Griswold, J. L. Martin, O. L. Welsh, D. M. Sutherland, L. A. Silva, T. S. Dermody

This study evaluates a Chikungunya virus vaccine candidate with synergistic mutations that enhance safety and induce neutralizing antibodies in mice.

bioRxiv · Oct 19, 2021Microbiology

The human neuronal receptor NgR1 bridges reovirus capsid proteins to initiate infection

D. M. Sutherland, M. Strebl, M. Koehler, O. L. Welsh, X. Yu, L. Hu, R. dos Santos Natividade, J. J. Knowlton, G. M. Taylor, R. Moreno, P. Woerz, Z. L. Lonergan, P. Aravamudhan, C. Guzman-Cardozo, D. Alsteens, , T. S. Dermody

This study identifies how NgR1 bridges reovirus capsid proteins to initiate infection, revealing a unique binding interface and its role in virus entry and receptor ligand interactions.

bioRxiv · Jul 23, 2021 · PreprintMicrobiology

The multi-functional reovirus σ3 protein is a virulence factor that suppresses stress granule formation to allow viral replication and myocardial injury

Y. Guo, M. M. Hinchman, M. Lewandrowski, S. T. Cross, D. M. Sutherland, O. L. Welsh, T. S. Dermody, J. S. L. Parker

This study identifies σ3 as a reovirus virulence factor that suppresses PKR activation and stress granule formation, linking these functions to viral replication and myocardial injury in mice.

bioRxiv · Mar 22, 2021Microbiology