Decoding protein networks during virus entry by quantitative proteomics

Bruening, Janina; Pietschmann, Thomas

doi:10.1016/j.virusres.2015.09.006

Cited by 28 publications

(18 citation statements)

References 156 publications

(180 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Pathogens engage host cell protein networks to gain access into replication competent intracellular compartments [21][22][23]. Mass spectrometry based-proteomics has matured into a powerful technology to comprehensively analyze protein-protein interactions (PPIs) from cell culture and primary cell material [22][23][24]. Here we set out to apply label-free quantitative (LFQ) proteomics to map the interaction network of the HCV and Plasmodium entry factor CD81 in human liver cells ( Fig 1A).…”

Section: Quantitative Proteomics Identifies 30 Cd81 Receptor Interactmentioning

confidence: 99%

Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB

et al. 2018

Self Cite

View full text Add to dashboard Cite

Hepatitis C virus (HCV) and the malaria parasite Plasmodium use the membrane protein CD81 to invade human liver cells. Here we mapped 33 host protein interactions of CD81 in primary human liver and hepatoma cells using high-resolution quantitative proteomics. In the CD81 protein network, we identified five proteins which are HCV entry factors or facilitators including epidermal growth factor receptor (EGFR). Notably, we discovered calpain-5 (CAPN5) and the ubiquitin ligase Casitas B-lineage lymphoma proto-oncogene B (CBLB) to form a complex with CD81 and support HCV entry. CAPN5 and CBLB were required for a post-binding and pre-replication step in the HCV life cycle. Knockout of CAPN5 and CBLB reduced susceptibility to all tested HCV genotypes, but not to other enveloped viruses such as vesicular stomatitis virus and human coronavirus. Furthermore, Plasmodium sporozoites relied on a distinct set of CD81 interaction partners for liver cell entry. Our findings reveal a comprehensive CD81 network in human liver cells and show that HCV and Plasmodium highjack selective CD81 interactions, including CAPN5 and CBLB for HCV, to invade cells.

show abstract

Section: Quantitative Proteomics Identifies 30 Cd81 Receptor Interactmentioning

confidence: 99%

Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB

et al. 2018

Self Cite

View full text Add to dashboard Cite

show abstract

“…In addition to the development of glycan array technologies, the field of virology has in the past decade benefited from advances in mass spectrometry-based proteomics. In particular shotgun proteomics, which is the unbiased detection of all proteins in a given biological sample, holds great promise for the identification of host factors of viral infection [132][133][134]. The basic principle of shotgun proteomics is the digestion of all proteins in a mixture with a defined enzyme such as trypsin and the subsequent identification of proteins based on their characteristic peptide fingerprint, for example, tryptic peptides unique to one protein in the whole proteomic space of a given species.…”

Section: Shotgun Proteomicsmentioning

confidence: 99%

“…Previously, AE-MS has successfully identified host factor interactions with viral non-structural proteins of virus families ranging from flaviviruses to herpesviruses (reviewed in Refs. [133,[147][148][149]). The application to virus receptor discovery is now in reach (Fig.…”

Section: Shotgun Proteomicsmentioning

confidence: 99%

Glycomics and Proteomics Approaches to Investigate Early Adenovirus–Host Cell Interactions

Laßwitz

Chandra

Arnberg

2018

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

Adenoviruses as most viruses rely on glycan and protein interactions to attach to and enter susceptible host cells. The Adenoviridae family comprises more than 80 human types and they differ in their attachment factor and receptor usage, which likely contributes to the diverse tropism of the different types. In the past years, methods to systematically identify glycan and protein interactions have advanced. In particular sensitivity, speed and coverage of mass spectrometric analyses allow for high-throughput identification of glycans and peptides separated by liquid chromatography. Also, developments in glycan microarray technologies have led to targeted, high-throughput screening and identification of glycan-based receptors. The mapping of cell surface interactions of the diverse adenovirus types has implications for cell, tissue, and species tropism as well as drug development. Here we review known adenovirus interactions with glycan- and protein-based receptors, as well as glycomics and proteomics strategies to identify yet elusive virus receptors and attachment factors. We finally discuss challenges, bottlenecks, and future research directions in the field of non-enveloped virus entry into host cells.

show abstract

“…In summary, despite the description of some receptors and entry factors of flavi-and hepaciviruses through genetic methods, secondary PPIs, the composition of cell surface receptor complexes, endocytosis complexes and fusion mechanisms are to a large extent unknown today. This calls for the application of the current highly sensitive and high-throughput compatible quantitative interaction proteomics methods to draw a clearer picture of the molecular events during host cell penetration by members of the Flaviviridae family (125).…”

Section: Zikvmentioning

confidence: 99%

Protein Interactions during the Flavivirus and Hepacivirus Life Cycle

Gerold

Bruening

Weigel

et al. 2017

Molecular & Cellular Proteomics

Self Cite

View full text Add to dashboard Cite

Protein-protein interactions govern biological functions in cells, in the extracellular milieu, and at the border between cells and extracellular space. Viruses are small intracellular parasites and thus rely on protein interactions to produce progeny inside host cells and to spread from cell to cell. Usage of host proteins by viruses can have severe consequences apoptosis, metabolic disequilibria, or altered cell proliferation and mobility. Understanding protein interactions during virus infection can thus educate us on viral infection and pathogenesis mechanisms. Moreover, it has led to important clinical translations, including the development of new therapeutic and vaccination strategies. Here, we will discuss protein interactions of members of the family, which are small enveloped RNA viruses. Dengue virus, Zika virus and hepatitis C virus belong to the most prominent human pathogenic With a genome of roughly ten kilobases encoding only ten viral proteins, display intricate mechanisms to engage the host cell machinery for their purpose. In this review, we will highlight how dengue virus, hepatitis C virus, Japanese encephalitis virus, tick-borne encephalitis virus, West Nile virus, yellow fever virus, and Zika virus proteins engage host proteins and how this knowledge helps elucidate infection. We will specifically address the protein composition of the virus particle as well as the protein interactions during virus entry, replication, particle assembly, and release from the host cell. Finally, we will give a perspective on future challenges in interaction proteomics and why we believe these challenges should be met.

show abstract

Decoding protein networks during virus entry by quantitative proteomics

Cited by 28 publications

References 156 publications

Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB

Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB

Glycomics and Proteomics Approaches to Investigate Early Adenovirus–Host Cell Interactions

Protein Interactions during the Flavivirus and Hepacivirus Life Cycle

Contact Info

Product

Resources

About