Angela Pearson

Areas of expertise

Molecular virology and viral pathogenesis

Professor

Phone
450-687-5010

Fax
450 686-5501

E-mail
angela.pearson@inrs.ca

Armand-Frappier Santé Biotechnologie Research Centre

531 des Prairies Blvd.
Laval, Quebec H7V 1B7
CANADA

See the research centre

Biography Ongoing research programmes Chairs, groups and networks

Professor Angela Pearson obtained her B.Sc. in Microbiology and Immunology from McGill University, and her Ph.D. in Molecular and Medical Genetics from the University of Toronto. After a postdoctoral fellowship in virology in the Department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School, Dr. Pearson joined the faculty at INRS-Institut Armand-Frappier in 2004. She is a former Research Scholar of the Fonds de recherche du Québec - Santé. She is an Associate Professor in the research axe of Infectious diseases, immunity, cancer, and epidemiology. Research in her group is focused on the biology of herpesviruses including the human pathogen herpes simplex virus (HSV) and the veterinary pathogen Canid herpesvirus 1 (CHV-1). HSV infections can be particularly harmful to those with weakened immune systems such as immunosuppressed transplant recipients or those living with AIDS, as well as to newborns due to their immature immune system. In her laboratory, a combination of molecular and cell biological strategies are used to address the following research aims:

to elucidate the role of viral genes, in particular the highly conserved UL24 gene, in HSV replication and pathogenesis;
to understand the the role of nucleolar proteins during HSV infection. The laboratory has shown that the nucleolar protein Upstream Binding Factor (UBF) inhibits HSV replication.
to understand the the replication mechanisms of CHV-1

Present work is aimed at understanding the mechanisms involved and at identifying the viral protein(s) that counter UBFs inhibitory activity to allow viral replication in the presence of UBF. The laboratory's research program on CHV-1 is focused on understanding virus-host cell interaction. In particular, work is aimed at identifying the entry pathways for CHV-1 into host cells as well as understanding the impact of CHV-1 on cellular miRNAs of the host. Professor Pearson is a member of the Centre of Excellence in Orphan Disease Research - Courtois Foundation (CERMO-FC).https://www.cermofc.uqam.ca/ Research in her laboratory is funded by grants from the National Sciences and Engineering Research Council of Canada (NSERC), the Canadian Institutes of Health Research (CIHR), and the Canada Foundation for Innovation (CFI).

Groups and networks

Professor Angela Pearson is a member of the Centre d'excellence en recherche sur les maladies orphelines -- Fondation Courtois (CERMO-FC). https://www.cermofc.uqam.ca/ Professor Angela Pearson is a member of the Réseau intersectoriel de recherche en sant de l’Université du Québec (RISUQ) https://www.risuq.uquebec.ca

Publications

Identification of glycosylated nucleosides in small synthetic glyco-RNAs.

St Michael F, Ben Hamouda M, Stupak J, Li J, Pearson A, Sauvageau J. Chembiochem. 2023 Dec 20:e202300784. doi: 10.1002/cbic.202300784. Online ahead of print.

The Disruption of a Nuclear Export Signal in the C-Terminus of the Herpes Simplex Virus 1 Determinant of Pathogenicity UL24 Protein Leads to a Syncytial Plaque Phenotype. Gonzalez CE, Ben Abdeljelil N, Pearson A. Viruses. 2023 Sep 21;15(9):1971. doi: 10.3390/v15091971.

Canid herpesvirus 1 Preferentially Infects Polarized Madin-Darby Canine Kidney Cells from the Basolateral Surface.

Eisa M, Micky S, Pearson A. Viruses. 2022 Jun 14;14(6):1291. doi: 10.3390/v14061291.

Entry of the Varicellovirus Canid herpesvirus 1 into Madin-Darby canine kidney epithelial cells is pH-independent and occurs via a macropinocytosis-like mechanism but without increase in fluid uptake.

Eisa M, Loucif H, van Grevenynghe J, Pearson A. Cell Microbiol. 2021 Dec;23(12):e13398. doi: 10.1111/cmi.13398. Epub 2021 Nov 15.

Editor’s choice: Cover image https://onlinelibrary.wiley.com/doi/10.1111/cmi.13401

Rel-Dependent Immune and Central Nervous System Mechanisms Control Viral Replication and Inflammation during Mouse Herpes Simplex Encephalitis.
Mancini M, Caignard G, Charbonneau B, Dumaine A, Wu N, Leiva-Torres GA, Gerondakis S, Pearson A, Qureshi ST, Sladek R, Vidal SM.
J Immunol. 2019 Mar 1;202(5):1479-1493. doi: 10.4049/jimmunol.1800063. Epub 2019 Jan 25.

A Mutation in the UL24 Gene Abolishes Expression of the Newly Identified UL24.5 Protein of Herpes Simplex Virus 1 and Leads to an Increase in Pathogenicity in Mice.
Dridi S, Richerioux N, Gonzalez Suarez CE, Vanharen M, Sanabria-Solano C, Pearson A.
J Virol. 2018 Sep 26;92(20). pii: e00671-18. doi: 10.1128/JVI.00671-18. Print 2018 Oct 15.

Herpes simplex virus 1 infection of T cells causes VP11/12-dependent phosphorylation and degradation of the cellular protein Dok-2.
Lahmidi S, Strunk U, Smiley JR, Pearson A, Duplay P.
Virology. 2017 Aug 22;511:66-73. doi: 10.1016/j.virol.2017.08.018. [Epub ahead of print].

Dok-1 and Dok-2 Are Required To Maintain Herpes Simplex Virus 1-Specific CD8⁺ T Cells in a Murine Model of Ocular Infection.
Lahmidi S, Yousefi M, Dridi S, Duplay P, Pearson A.
J Virol. 2017 Jul 12;91(15). pii: e02297-16. doi: 10.1128/JVI.02297-16. Print 2017 Aug 1.

Herpes Simplex Virus 1 UL24 Abrogates the DNA Sensing Signal Pathway by Inhibiting NF-κB Activation.
Xu H, Su C, Pearson A, Mody CH, Zheng C.
J Virol. 2017 Mar 13;91(7). pii: e00025-17. doi: 10.1128/JVI.00025-17. Print 2017 Apr 1.

Regulation of viral gene expression by the herpes simplex virus 1 UL24 protein (HSV-1UL24 inhibits accumulation of viral transcripts).
Sanabria-Solano C, Gonzalez CE, Richerioux N, Bertrand L, Dridi S, Griffiths A, Langelier Y, Pearson A.
Virology. 2016 Aug;495:148-60. doi: 10.1016/j.virol.2016.05.006. Epub 2016 May 20.

Mutation of UL24 impedes the dissemination of acute herpes simplex virus 1 infection from the cornea to neurons of trigeminal ganglia.
Rochette PA, Bourget A, Sanabria-Solano C, Lahmidi S, Lavallée GO, Pearson A.
J Gen Virol. 2015 Sep;96(9):2794-805. doi: 10.1099/vir.0.000189. Epub 2015 May 18.

Upstream binding factor inhibits herpes simplex virus replication.
Ouellet Lavallée G, Pearson A.
Virology. 2015 Sep;483:108-16. doi: 10.1016/j.virol.2015.04.003. Epub 2015 May 15.

Visualization of mouse neuronal ganglia infected by Herpes Simplex Virus 1 (HSV-1) using multimodal non-linear optical microscopy.
Rochette PA, Laliberté M, Bertrand-Grenier A, Houle MA, Blache MC, Légaré F, Pearson A.
PLoS One. 2014 Aug 18;9(8):e105103. doi: 10.1371/journal.pone.0105103. eCollection 2014.

Genome-wide mouse mutagenesis reveals CD45-mediated T cell function as critical in protective immunity to HSV-1.
Caignard G, Leiva-Torres GA, Leney-Greene M, Charbonneau B, Dumaine A, Fodil-Cornu N, Pyzik M, Cingolani P, Schwartzentruber J, Dupaul-Chicoine J, Guo H, Saleh M, Veillette A, Lathrop M, Blanchette M, Majewski J, Pearson A, Vidal SM.
PLoS Pathog. 2013 Sep;9(9):e1003637. doi: 10.1371/journal.ppat.1003637. Epub 2013 Sep 12.

The UL24 protein of herpes simplex virus 1 affects the sub-cellular distribution of viral glycoproteins involved in fusion.
Ben Abdeljelil N, Rochette PA, Pearson A.
Virology. 2013 Sep;444(1-2):263-73. doi: 10.1016/j.virol.2013.06.021. Epub 2013 Jul 20.

The Ribonucleotide Reductase R1 Subunits of Herpes Simplex Virus 1 and 2 Protect Cells against Poly(I {middle dot} C)-Induced Apoptosis.
Dufour F, Bertrand L, Pearson A, Grandvaux N, Langelier Y.
J Virol. 2011 Sep;85(17):8689-701. Epub 2011 Jun 22.

Involvement of the UL24 protein in herpes simplex virus 1-induced dispersal of B23 and in nuclear egress.
Lymberopoulos MH, Bourget A, Ben Abdeljelil N, Pearson A.
Virology. 2011 Apr 10;412(2):341-8. Epub 2011 Feb 12.

Relocalization of upstream binding factor to viral replication compartments is UL24 independent and follows the onset of herpes simplex virus 1 DNA synthesis.
Lymberopoulos MH, Pearson A.
J Virol. 2010 May;84(9):4810-5. Epub 2010 Feb 10.

Differential importance of highly conserved residues in UL24 for herpes simplex virus 1 replication in vivo and reactivation.
Leiva-Torres GA, Rochette PA, Pearson A.
J Gen Virol. 2010 May;91(Pt 5):1109-16. Epub 2010 Jan 13.

Conserved residues in the UL24 protein of herpes simplex virus 1 are important for dispersal of the nucleolar protein nucleolin.
Bertrand L, Leiva-Torres GA, Hyjazie H, Pearson A.
J Virol. 2010 Jan;84(1):109-18. Epub.

The conserved N-terminal domain of herpes simplex virus 1 UL24 protein is sufficient to induce the spatial redistribution of nucleolin.
Bertrand L, Pearson A.
J Gen Virol. 2008 May;89(Pt 5):1142-51.(Figure de l’article choisie pour la page couverture de la revue.)

Involvement of UL24 in herpes-simplex-virus-1-induced dispersal of nucleolin.
Lymberopoulos MH, Pearson A.
Virology. 2007 Jul 5;363(2):397-409. Epub 2007 Mar 7.

Phosphorylation of the RNA polymerase II carboxyl-terminal domain in human cytomegalovirus-infected cells and in vitro by the viral UL97 protein kinase.
Baek MC, Krosky PM, Pearson A, Coen DM.
Virology. 2004 Jun 20;324(1):184-93.

ICP27 selectively regulates the cytoplasmic localization of a subset of viral transcripts in herpes simplex virus type 1-infected cells.
Pearson A, Knipe DM, Coen DM.
J Virol. 2004 Jan;78(1):23-32.

Failure of thymidine kinase-negative herpes simplex virus to reactivate from latency following efficient establishment.
Chen SH, Pearson A, Coen DM, Chen SH.
J Virol. 2004 Jan;78(1):520-3.

Identification, localization, and regulation of expression of the UL24 protein of herpes simplex virus type 1.
Pearson A, Coen DM.
J Virol. 2002 Nov;76(21):10821-8.

Activation of the murine dihydrofolate reductase promoter by E2F1. A requirement for CBP recruitment.
Fry CJ, Pearson A, Malinowski E, Bartley SM, Greenblatt J, Farnham PJ.
J Biol Chem. 1999 May 28;274(22):15883-91.

Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH.
Pearson A, Greenblatt J.
Oncogene. 1997 Nov 27;15(22):2643-58.

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.
Xiao H, Pearson A, Coulombe B, Truant R, Zhang S, Regier JL, Triezenberg SJ, Reinberg D, Flores O, Ingles CJ, et al.
Mol Cell Biol. 1994 Oct;14(10):7013-24.

The 5′ noncoding region sequence of the Choristoneura biennis entomopoxvirus spheroidin gene functions as an efficient late promoter in the mammalian vaccinia expression system.
Pearson A, Richardson C, Yuen L.
Virology. 1991 Feb;180(2):561-6.