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26 results on '"Lennemann, Nicholas J."'

16. Vesicular Stomatitis Virus Pseudotyped with Ebola Virus Glycoprotein Serves as a Protective, Noninfectious Vaccine against Ebola Virus Challenge in Mice

Author

Lennemann, Nicholas J., primary, Herbert, Andrew S., additional, Brouillette, Rachel, additional, Rhein, Bethany, additional, Bakken, Russell A., additional, Perschbacher, Katherine J., additional, Cooney, Ashley L., additional, Miller-Hunt, Catherine L., additional, Ten Eyck, Patrick, additional, Biggins, Julia, additional, Olinger, Gene, additional, Dye, John M., additional, and Maury, Wendy, additional

Published
2017
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25. Modification of N-Linked Glycan Sites in Viral Glycoproteins.

Author

Lennemann NJ, Corliss L, and Maury W

Subjects
Glycosylation, Protein Processing, Post-Translational, Glycoproteins chemistry, Polysaccharides chemistry
Abstract

Post-translational modification of proteins by the addition of sugar chains, or glycans, is a functionally important hallmark of proteins trafficked through the secretory system. These proteins are termed glycoproteins. Glycans are known to be important for initiating signaling through binding of cell surface receptors, facilitating protein folding, and maintaining protein stability. For pathogens, glycans can also mask vulnerable protein regions from neutralizing antibodies. Thus, there is a need to develop methods to decipher the role of specific glycans attached to proteins in order to understand their biological role. Here, we describe established methods for identifying glycosylated residues and understanding their role in protein synthesis and function using viral glycoproteins as a model., (© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)

Published
2024
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26. BPIFB3 interacts with ARFGAP1 and TMED9 to regulate non-canonical autophagy and RNA virus infection.

Author

Evans AS, Lennemann NJ, and Coyne CB

Subjects
Animals, Endoplasmic Reticulum, Virus Replication, Autophagy, RNA Virus Infections
Abstract

Autophagy is a degradative cellular pathway that targets cytoplasmic contents and organelles for turnover by the lysosome. Various autophagy pathways play key roles in the clearance of viral infections, and many families of viruses have developed unique methods for avoiding degradation. Some positive-stranded RNA viruses, such as enteroviruses and flaviviruses, usurp the autophagic pathway to promote their own replication. We previously identified the endoplasmic reticulum (ER)-localized protein BPIFB3 as an important negative regulator of non-canonical autophagy that uniquely impacts the replication of enteroviruses and flaviviruses. Here, we find that many components of the canonical autophagy machinery are not required for BPIFB3 depletion-induced autophagy and identify the host factors that facilitate its role in the replication of enteroviruses and flaviviruses. Using proximity-dependent biotinylation (BioID) followed by mass spectrometry, we identify ARFGAP1 and TMED9 as two cellular components that interact with BPIFB3 to regulate autophagy and viral replication. Importantly, our data demonstrate that non-canonical autophagy in mammalian cells can be controlled outside of the traditional pathway regulators and define the role of two proteins in BPIFB3 depletion mediated non-canonical autophagy., Competing Interests: Competing interestsThe authors declare no competing or financial interests., (© 2021. Published by The Company of Biologists Ltd.)

Published
2021
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