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Dr Jeremy Rossman

Senior Lecturer in Virology

School of Biosciences

 

Dr Jeremy Rossman joined the School of Biosciences in November 2011 as a Lecturer in Virology. He received a Ph.D. in Emerging Infectious Diseases from the Uniformed Services University of the Health Sciences (Bethesda, Maryland, USA) for his studies on T lymphocyte signal transduction (2006). Following his Ph.D., he conducted postdoctoral research with Prof. Robert Lamb at the Howard Hughes Medical Institute (Northwestern University, Evanston, Illinois, USA) where he investigated the mechanisms of influenza virus budding (2006-2011). His current research focuses on host-pathogen interactions of negative sense RNA viruses and interdisciplinary research on public health and humanitarian aid.

Jeremy is a member of the Microbial Pathogenesis Group.

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Also view these in the Kent Academic Repository

Article
Cantoni, D. and Rossman, J. (2018). Ebolaviruses: New roles for old proteins. PLOS Neglected Tropical Diseases [Online] 12:e0006349. Available at: https://doi.org/10.1371/journal.pntd.0006349.
Perot, B. et al. (2018). Autophagy diminishes the early interferon- β response to influenza A virus resulting in differential expression of interferon- stimulated genes. Cell death & disease [Online]. Available at: http://dx.doi.org/10.1038/s41419-018-0546-5.
Calnan, M. et al. (2017). The response to and impact of the Ebola epidemic: towards an agenda for interdisciplinary research. International Journal of Health Policy and Management [Online] 7:402-411. Available at: http://dx.doi.org/10.15171/ijhpm.2017.104.
Pappalardo, M. et al. (2017). Changes associated with Ebola virus adaptation to novel species. Bioinformatics [Online] 33:1911-1915. Available at: http://dx.doi.org/10.1093/bioinformatics/btx065.
Saintas, E. et al. (2017). Acquired resistance to oxaliplatin is not directly associated with increased resistance to DNA damage in SK-N-ASrOXALI4000, a newly established oxaliplatin-resistant sub-line of the neuroblastoma cell line SK-N-AS. PloS one [Online] 12:e0172140. Available at: http://dx.doi.org/10.1371/journal.pone.0172140.
Martyna, A. et al. (2017). Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission. Scientific Reports [Online]. Available at: http://dx.doi.org/10.1038/srep44695.
Saintas, E. et al. (2017). Acquired resistance to oxaliplatin is not directly associated with increased resistance to DNA damage in SK-N-ASrOXALI4000, a newly established oxaliplatin-resistant sub-line of the neuroblastoma cell line SK-N-AS. PLoS ONE [Online] 12:e0172140. Available at: http://dx.doi.org/10.1371/journal.pone.0172140.
Badham, M. and Rossman, J. (2016). Filamentous Influenza Viruses. Current Clinical Microbiology Reports [Online] 3:155-161. Available at: http://dx.doi.org/10.1007/s40588-016-0041-7.
Qian, Z. et al. (2016). Discovery and Mechanism of Highly Efficient Cyclic Cell-Penetrating Peptides. Biochemistry [Online]:1-1. Available at: http://dx.doi.org/10.1021/acs.biochem.6b00226.
Cantoni, D. et al. (2016). Risks Posed by Reston, the Forgotten Ebolavirus. mSphere [Online] 1. Available at: http://dx.doi.org/10.1128/mSphere.00322-16.
Zhirnov, O. et al. (2016). Intravirion cohesion of matrix protein M1 with ribonucleocapsid is a prerequisite of influenza virus infectivity. Virology [Online] 492:187-196. Available at: http://dx.doi.org/10.1016/j.virol.2016.02.021.
Wass, M., Rossman, J. and Michaelis, M. (2016). Ebola outbreak highlights the need for wet and dry laboratory collaboration. Journal of Virology and Emerging Diseases [Online] 2. Available at: http://dx.doi.org/10.16966/2473-1846.e102.
Martyna, A. et al. (2016). Curvature Sensing by a Viral Scission Protein. Biochemistry [Online]. Available at: http://dx.doi.org/10.1021/acs.biochem.6b00539.
Shagari, H. et al. (2016). The 2014 Ebola Outbreak: Preparedness in West African Countries and its Impact on the Size of the Outbreak. Journal of Emerging Diseases and Virology [Online] 2. Available at: http://dx.doi.org/10.16966/2473-1846.123.
Pappalardo, M. et al. (2016). Conserved differences in protein sequence determine the human pathogenicity of Ebolaviruses. Scientific reports [Online] 6:23743. Available at: http://dx.doi.org/10.1038/srep23743.
Rossman, J. and Martyna, A. (2014). Alterations of membrane curvature during influenza virus budding. Biochemical Society Transactions [Online] 42:1425-1428. Available at: http://dx.doi.org/10.1042/BST20140136.
da Silva, D. et al. (2014). The Influenza Virus Neuraminidase Protein Trans-membrane and Head Domains Have Coevolved. Journal of Virology [Online] 89:1094-1104. Available at: http://dx.doi.org/10.1128/JVI.02005-14.
Rossman, J. and Lamb, R. (2013). Viral Membrane Scission. Annual Review of Cell and Developmental Biology [Online] 29:551-569. Available at: http://www.annualreviews.org/doi/abs/10.1146/annurev-cellbio-101011-155838?journalCode=cellbio.
Rossman, J., Leser, G. and Lamb, R. (2012). Filamentous Influenza Virus Enters Cells via Macropinocytosis. Journal of Virology [Online] 86:10950-10960. Available at: http://dx.doi.org/10.1128/JVI.05992-11.
Rossman, J. and Lamb, R. (2011). Influenza virus assembly and budding. Virology 411:229-36.
Rossman, J. et al. (2010). Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation. Journal of Virology [Online] 84:5078-5088. Available at: http://dx.doi.org/10.1128/JVI.00119-10.
Rossman, J. and Lamb, R. (2010). Swine-origin Influenza Virus and the 2009 Pandemic. American Journal of Respiratory and Critical care Medicine [Online] 181:295-296. Available at: http://dx.doi.org/10.1164/rccm.200912-1876ED.
Rossman, J. et al. (2010). Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission. Cell [Online] 142:902-913. Available at: http://dx.doi.org/10.1016/j.cell.2010.08.029.
Rossman, J. and Lamb, R. (2009). Autophagy, apoptosis, and the influenza virus M2 protein. Cell Host & Microbe [Online] 6:299-300. Available at: http://dx.doi.org/10.1016/j.chom.2009.09.009.
Langel, F. et al. (2008). Multiple protein domains mediate interaction between Bcl10 and MALT1. Journal of Biological Chemistry [Online] 283:32419-31. Available at: http://dx.doi.org/10.1074/jbc.M800670200.
Rossman, J. et al. (2006). POLKADOTS are foci of functional interactions in T-Cell receptor-mediated signaling to NF-kappaB. Molecular Biology of the Cell [Online] 17:2166-76. Available at: http://dx.doi.org/10.1091/mbc.E05-10-0985.
Total publications in KAR: 26 [See all in KAR]

 

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The overall goal of our laboratory is to identify key interactions that regulate viral replication, determine the biophysical mechanics that underlay these reactions and place these reactions in the context of the host cell in order to better understand the larger context of host-pathogen interactions and fundamental cell biology. Current research is focused on the host-pathogen interactions governing the replication of negative sense RNA viruses, including Influenza A virus, respiratory syncytial virus and Ebola virus. From these interactions we are interrogating multiple stages of viral replication ranging from viral assembly and budding to interactions with the host immune system.  These processes are being investigated using a broad range of state-of-the-art methodologies, including: super-resolution microscopy, cryo-TEM, single molecule imaging, neutron reflectivity, solution NMR, lipidomics, molecular dynamics simulations and machine learning algorithms, with the goal of opening new avenues for drug discovery, vaccine development and ultimately the treatment and prevention of these viral diseases.

Mechanisms of Influenza virus assembly and budding

budding

The influenza virus is a continually emerging pathogen capable of causing high rates of morbidity and mortality and exacting significant socio-economic costs. Influenza epidemics occur with seasonal regularity; however, influenza viruses also dominate the headlines with new and dangerous variations such as 'swine flu' and 'avian influenza'.  Yet despite the prevalence and widespread effects of influenza viruses, there are no universal vaccines and precious few therapeutic agents. 

Among the least understood events of the influenza virus lifecycle are the processes that mediate the formation of new viruses and their release from the host cell by membrane fission. Recently we have found a novel role for the influenza virus M2 protein in virus budding, the mediation of membrane fission. The aim of this research is to investigate the structure and function of the influenza virus M2 protein to better understand its involvement in virus budding, and to utilize that knowledge in the design of novel therapeutic agents targeting influenza virus assembly and budding.

Our research on IAV budding is funded by the Medical Research Council and the European Commission.

Examination of the functional significance of filamentous viral morphology

morphology

Influenza viruses (and other negative sense RNA viruses, including Ebola virus and respiratory syncytial virus) exist in two distinct morphological forms, filamentous and spherical virions, although the significance of these morphologies is unknown.  Previous evidence suggests that the filamentous form may be the dominant morphology produced during human infections, in contrast to the standard laboratory strains, which appear predominantly spherical.  Our lab is investigating the mechanism of filamentous virion assembly and the functional significance of viral morphology, its relevance to human disease and its possible exploitation in the development of novel therapeutic agents.

Our research on IAV morphology is funded by the Medical Research Council and MedImmune.

Interdisciplinary examination of the response to, and impact of, the 2014 Ebola virus epidemic

The 2013-16 Ebola virus disease (EVD) epidemic in West Africa was the largest in history and resulted in a huge public health burden and significant social and economic impact in those countries most affected. Its size, duration and geographical spread presents important opportunities for research than might help national and global health and social care systems to better prepare for and respond to future outbreaks. We are currently investigating the research needs and priorities from the perspective of those who directly experienced the EVD epidemic in Guinea. This is a collaborative project between the School of Biosciences, the School of Social Policy, Sociology and Social Research, Public Health England and the FOSAD Health and Sustainable Development Foundation of Guinea.

Ebola virus pathogenicity and immune evasion

Ebola virus is one of the most deadly pathogens known, with many strains causing 60-90% case-fatality rates, such as seen in the recent 2014 West Africa Ebola virus outbreak. However, the Ebola virus Reston strain is not known to cause any human disease and has a 0% case-fatality rate. In collaboration with the University of Manitoba and the Canadian Food Inspection Agency we are investigating the mechanisms underlying this dramatic difference in pathogenicity.

Using global data to identify hotspots for newly emerging infectious diseases

The past 20 years have seen the emergence of multiple new pathogenic viruses around the world. In collaboration with the School of Computing, we are determining the pre-existing ecological, meteorological, geological and socioeconomic factors that correlate with the emergence of novel infectious viral diseases. These factors will then by analyzed using cutting-edge machine learning algorithms in order to predict hotspots for the next emerging viral disease, thus facilitating enhanced surveillance and rapid containment.

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Postdoctoral Research Associates

  • Dr Basma Bahsoun

 

Ph.D. Students

  • Nafisa Huq
  • Diego Cantoni
  • Matthew Badham (MRC Industrial CASE Studentship)
  • Joseph Bore (with Public Health England)

 

MSc Research Students

  • Rebecca Steventon

 

Former Students

  • Dr Agnieszka Martyna (PhD)
  • Frederic Jackson (MSc)
  • Rebecca Clark (MSc)
  • Towseef Ahmad (MSc with Chemistry)
  • Matthew Badham (MSc)
  • Alex Atkins (MSc)
  • Christopher Wilson (MSc)
  • Scott Roddy (MSc)

 

Applications will be considered from self-funded students and from postdoctoral researchers intent on securing their own fellowship.

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Final Year

  • BI606 Pathogens & Pathogenicity
  • BI620 Virology (module convenor)
  • BI622 Advanced Immunology

 

MSc in Infectious Diseases

  • BI856 Viral Pathogens (module convenor)

 

School of Biosciences Press Officer

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Enquiries: Phone: +44 (0)1227 823743

School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ

Last Updated: 23/04/2018