- 2012: Instructor. Department of Medicine. Harvard Medical School
- 2008: Postdoctoral Research Fellow. Department of Microbiology and Immunobiology. Harvard Medical School
- 2007: Ph.D. Microbiology. University of Barcelona. Spain
- 2005: M.S. Advanced Microbiology and Biotechnology. University of Barcelona. Spain
- 2003: B.S. Biology. University of Barcelona. Spain
MBIO 4310 / BIOL 6301-006: Introduction to Virology (Fall).
BIOL 4301 / BIOL 6301-006: Special topics in Biology: Virology II (Spring)
The research studies in my lab are focused on understanding the mechanisms by which Human Immunodeficiency Virus (HIV), and its close relative Simian Immunodeficiency Virus (SIV) circumvent the barriers of the innate immunity in their respective hosts, and cause Acquired Immunodeficiency Syndrome (AIDS). We are particularly interested in the mechanisms by which HIV and SIV overcome restriction by Tetherin/BST2, BCA2 and autophagy.
Tetherin is an integral membrane protein that traps nascent virions to the plasma membrane, thereby, impeding their release and spread. We demonstrated that SIV uses its Nef accessory protein to overcome restriction by non-human primate Tetherin, and this is achieved by targeting a five amino-acid motif in this protein. However, human Tetherin lacks this motif, making Nef unable to counteract the antiviral effects of Tetherin in humans. As a consequence of this, HIV-1 and HIV-2 needed to evolve alternative mechanisms to circumvent the Tetherin block. In particular, HIV-1 uses its accessory protein Vpu, while HIV-1 uses Env to remove human Tetherin from sites of virion assembly. These observations highlight the extraordinary plasticity of the primate lentiviruses to counteract Tetherin, and suggest that Tetherin constitutes a significant obstacle for infectivity and cross-species transmission.
BCA2 (Breast-Cancer Associated gene 2) is a co-factor in the restriction imposed by Tetherin on HIV. By interacting with Tetherin, BCA2 promotes the internalization and degradation of “tethered” virions. However, our lab demonstrated that BCA2 also has Tetherin-independent antiviral activity. Specifically, BCA2 promotes the lysosomal degradation of the HIV protein Gag (precursor of the viral matrix, capsid and nucleocapsid), thus, impairing virion assembly. Our most recent work shows that BCA2 is intimately connected with innate immune system, since it modulates the transcription factor NF-κB. NF-κB is normally activated in response to infections and other insults. However, HIV takes advantage of the activation of this pathway, and uses NF-κB to enhance the expression of its viral genes. BCA2, on the other hand, potently shuts down NF-κB signaling, impairing significantly virus gene expression and replication. Therefore, these observations provide additional mechanisms by which BCA2 represents a promising factor for antiretroviral therapy against HIV.
Autophagy is a highly conserved cellular response against stressful conditions such as viral infections. The role of autophagy in HIV infection is currently controversial. Some reports state that HIV activates autophagy to enhance infectivity, while others claim that HIV blocks specific steps in the autophagy machinery to prevent viral degradation. To bring light into this issue, we are currently investigating how autophagy affects HIV replication, and if HIV can modulate this innate response.
In addition to the research projects presented above, we are currently investigating (1) additional mechanisms of HIV restriction by Tetherin and BCA2; (2) the strategies used by HIV and SIV to circumvent these barriers; and (3) the association between BCA2 expression and cancer. Therefore, these goals are directly relevant in the development of novel antiretroviral drugs to enhance the containment of HIV replication by the innate immunity.
Ph.D. student position in virology: HIV-host interactions
Are you interested in pursuing a Ph.D. in a cutting-edge field? The laboratory of Dr. Ruth Serra-Moreno at Texas Tech University is recruiting a Ph.D. student to join her laboratory next academic year. The lab is looking for a talented, committed, hard-worker, self-driven and resourceful student interested in undertaking original, in-depth research project in the field of HIV-host interactions, with a particular focus on the crossroads between infection, innate immunity, and pulmonary vascular biology. This project is a collaborative effort between the Serra-Moreno's laboratory at TTU and Dr. Sharilyn Almodovar's lab at the Texas Tech University Health Sciences Center.
For additional information about the Almodovar lab, please visit:
- Hold a bachelor degree in biological sciences or related field
- Currently pursuing a Ph.D. degree in TTU
- Good communication and interpersonal skills
- Experience in molecular biology and cell culture is preferred.
Please send applications to Dr. Serra-Moreno at firstname.lastname@example.org. Please, include your CV, letter of motivation and the name of three references.
Colomer-Lluch, M. and Serra-Moreno R. 2017. BCA2/RABRING7 Interferes with HIV-1 Proviral Transcription by Enhancing the SUMOylation of IκBα. J Virol. 2017 March 29; 91(8).
Arias, J., Colomer-Lluch, M, von Bredow, B., Greene, J., MacDonald, J., O'Connor, D., Serra-Moreno, R., and Evans, D. 2016. Tetherin Antagonism by HIV-1 Group M Nef Proteins. J Virol. Sept. 2016 (JVI01465-16R1). PMID: 27654287
- Colomer-Lluch, M., Gollahon L.S. and Serra-Moreno R. 2016. Anti-HIV factors: targeting each step of HIV's replication cycle. Curr. HIV. Res. 2016; 14(3):175-182
Serra-Moreno, R. 2014. The end of Nef's tether. Trends Microbiol. Dec; 22(12):662-664. PMCID: PMC4258156.
Nityanandam, R. and Serra-Moreno, R. 2014. BCA2/Rabring7 targets HIV-1 Gag for lysosomal degradation in a tetherin-independent manner. PLoS Pathogens. May 22;10(5):e1004151.
- Serra-Moreno, R*., Zimmermann, K., Stern, L.J., and Evans, D.T. 2013. Tetherin/BST-2 Antagonism by Nef Depends on a Direct Physical Interaction between Nef and Tetherin, and on Clathrin-mediated Endocytosis. PLoS Pathogens. July;9(7):e1003487. *corresponding author
- Serra-Moreno, R., and Evans D.T. 2012. Adaptation of Human and Simian Immunodeficiency Viruses for Resistance to Tetherin/BST-2. Current HIV Research. Jun;10(4):277-82.
- Serra-Moreno, R., Jia, B., Breed, M., Alvarez, X., and Evans, D.T. 2011. Compensatory changes in gp41 restore resistance to tetherin in a pathogenic nef-deleted SIV. Cell Host & Microbe. Jan 20; 9(1): 46-57.
- Evans, D.T., Serra-Moreno, R., Singh, R.K., and Guatelli, J.C. 2010. BST2/Tetherin: a new component of the innate response to enveloped viruses. Trends Microbiol. Sep 18(9): 388-396.
- Jia, B*., Serra-Moreno, R*., Neidermyer, W., Rahmberg, A., Mackey, J., Fofana, I.B., Johnson, W.E., Westmoreland, S., and Evans, D. 2009. Species-specificity Activity of SIV Nef and HIV-1 Vpu in Overcoming Restriction by Tetherin/BST2. PLoS Pathog. May;5(5):e1000429. Epub 2009 May 15. *Both authors collaborated equally in this work.
- Serra-Moreno R., Jofre J. and Muniesa M. 2008. The CI repressors of Shiga toxin-converting prophages are involved in coinfection of Escherichia coli strains, which causes a down regulation in the production of Shiga toxin 2. J Bacteriol. Jul;190(13):4722-35. Epub 2008 May
- Serra-Moreno R., Jofre J. and Muniesa M. 2007. Insertion site occupancy by stx2 bacteriophages depends on the locus availability of the host strain chromosome. J Bacteriol. Sep;189(18):6645-54. Epub 2007 Jul 20.
- Serra-Moreno R., Acosta S., Hernalsteens J.P., Jofre J. and Muniesa M. 2006. Use of the lambda Red recombinase system to produce recombinant prophages carrying antibiotic resistance genes. BMC Mol Biol. Sep 19;7:31