Author

D. J. Goetschius

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

Biology Disciplines

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Microbiology· 2 Evolutionary Biology· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Research Focus:host-pathogen & immune response· 3 Approach:experimental assay· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Assay:cryo-EM· 1 Approach:deep learning· 1 Organism:human· 1

Frequent Co-Authors

C. M. Bator· 3 shared S. L. Hafenstein· 3 shared C. R. Parrish· 2 shared N. D. Christensen· 2 shared S. R. Hartmann· 2 shared A. E. Lukacher· 1 shared A. M. Makhov· 1 shared B. K. Alford· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersMicrobiology

C. M. Bator

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Viral capsid, antibody, and receptor interactions: experimental analysis of the antibody escape evolution of canine parvovirus

R. Lopez-Astacio, O. F. Adu, D. J. Goetschius, H. Lee, W. Weichert, B. R. Wasik, S. P. Frueh, B. K. Alford, I. E. H. Voorhees, J. F. Flint, S. Saddoris, L. B. Goodman, E. C. Holmes, S. Hafenstein, C. R. Parrish

This study uses in vitro selection and deep sequencing to identify escape mutations in canine parvovirus selected by two antibodies, revealing mechanisms of antibody and receptor binding interactions.

Journal of Virology · Jun 29, 2023Peer-reviewedEvolutionary Biology

Mechanisms of antibody binding revealed by asymmetric Fab-virus complexes

D. J. Goetschius, S. R. Hartmann, L. J. Organtini, H. Callaway, K. Huang, C. M. Bator, R. E. Ashley, A. M. Makhov, J. F. Conway, C. R. Parrish, S. L. Hafenstein

The paper uses cryo-EM to analyze antibody binding to parvovirus capsids, revealing structural insights into epitope-receptor interactions and species-specific neutralization.

bioRxiv · Dec 1, 2020 · PreprintMicrobiology

High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility

D. J. Goetschius, S. R. Hartmann, S. Subramanian, C. M. Bator, N. D. Christensen, S. L. Hafenstein

This study presents a high-resolution 3.1 Å structure of HPV16 using cryo-EM, identifies the minor structural protein L2, and reveals capsid flexibility through inter-capsomer analysis.

bioRxiv · Oct 27, 2020Microbiology

Antibody Escape by Polyomavirus Capsid Mutation Facilitates Neurovirulence

M. D. Lauver, D. J. Goetschius, C. S. Netherby-Winslow, K. N. Ayers, G. Jin, D. G. Haas, E. L. Frost, S. H. Cho, C. M. Bator, S. M. Bywaters, N. D. Christensen, S. L. Hafenstein, A. E. Lukacher

The paper shows a JCPyV-PML VP1 mutation enables antibody escape and neurovirulence in mice.

bioRxiv · Jul 14, 2020Immunology