Author

S. L. Hafenstein

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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Immunology· 2 Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

C. M. Bator· 3 shared D. J. Goetschius· 3 shared C. Bator· 2 shared N. D. Christensen· 2 shared S. R. Hartmann· 2 shared A. E. Kerr· 1 shared A. E. Lukacher· 1 shared A. M. Makhov· 1 shared

Activity by Year

2020-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersMicrobiology

C. M. Bator

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Intranasal SARS-CoV-2 RBD decorated nanoparticle vaccine enhances viral clearance in the Syrian hamster model

D. R. Patel, A. M. Minns, D. G. Sims, C. J. Field, A. E. Kerr, T. Heinly, E. H. Luley, R. M. Rossi, C. Bator, I. M. Mostafa, S. L. Hafenstein, S. E. Lindner, T. C. Sutton

This paper develops an intranasal nanoparticle vaccine against SARS-CoV-2 using a SpyCage scaffold decorated with RBD, showing enhanced viral clearance in Syrian hamsters without preventing infection.

bioRxiv · Oct 27, 2022Immunology

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

Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP

A. Perederina, D. Li, H. Lee, C. Bator, I. Berezin, S. L. Hafenstein, A. S. Krasilnikov

The paper reports a cryo-EM structure of the yeast RNase MRP complex, showing how its catalytic center and substrate binding pocket differ from RNase P due to RNA-driven protein remodeling.

bioRxiv · Mar 17, 2020Biochemistry