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Pamela Hall, PhD

Assistant Professor

Department of Pharmaceutical Sciences
Office: Multidisciplinary Research Facility (MF), room 208-9
Phone: 505.272.0915

Email  |  Curriculum Vitae | Laboratory Website


  • Ph.D. (Pharmacology) Case Western Reserve University, Cleveland, OH, 2004

  • M.S. (Molecular Biology) University of Alabama in Huntsville, 1999

  • B.S. (Microbiology) University of Alabama in Huntsville, 1989

Post Doctoral Training

2006-2008 Post-doctoral Fellow, University of New Mexico Health Sciences Center, Albuquerque, NM.
Peptide and small molecule inhibitors of Hantavirus infection, Innate immune response to Hantavirus infection

2005 Post-doctoral Fellow, NIDDK, National Institutes of Health, Bethesda, MD
Structural recognition of pathogenic ligands by TLRs

2004-2005 Post-doctoral Fellow, Department of Biochemistry, Case Western Reserve University, Cleveland, OH
Structural studies of the transcarboxylase enzyme complex 

Research Interests

Staphylococcus aureus bacteria commonly colonize a large percentage of the population. Historically known as an agent of nosocomial infection (hospital-acquired) in patients with predisposing health conditions, recent years have witnessed a dramatic rise in S. aureus infections in apparently healthy individuals in the community setting (community-acquired). Further complicating this problem, S. aureus has acquired resistance genes which protect the bacterium from frequently utilized methicillin-type antibiotics. These strains, known as methicillin-resistant Staphylococcus aureus (MRSA), are seen in both hospital-acquired (HA-MRSA) and community-acquired (CA-MRSA) infections. MRSA has recently been highlighted in the press due to its impact on both public health and on the added financial burden to patient care.

The rise in CA-MRSA infections is due to changes in virulence of strains causing the infections, but previously unidentified defects in innate defense mechanisms of otherwise healthy individuals may also contribute. In this regard, our lab is interested in understanding how our innate immune system defends us against invasive infection by S. aureus, particularly by CA-MRSA. S. aureus utilizes a peptide-pheromone based communication system, called quorum-sensing, to switch from an adherent colonizing phenotype to a virulent phenotype capable of causing invasive infection. The peptide pheromones responsible for signaling this change in virulence are referred to as autoinducing peptides or AIPs. It was recently demonstrated that apolipoprotein B (apoB), a component of both very-low density lipoprotein (VLDL) and low density lipoprotein (LDL) particles, can bind to AIPs and prevent the switch to an invasive bacterial phenotype. We are currently addressing the molecular mechanism by which apoB antagonizes quorum sensing. This information will provide insight into the role of this molecule as an innate defense protein and possibly provide clues to identification of therapeutic inhibitors of MRSA quorum sensing.

Selected Publications

Femling, J.K., West, S.D., Hauswald, E.K., Gresham, H.D. and P.R. Hall (2013). Nosocomial infections after severe trauma are associated with lower apolipoproteins B and AII. J Trauma Acute Care Surg. 74: 1067-73.

Hall, P.R., Elmore, B.O., Spang, C.H., Alexander, S.M., Manifold-Wheeler, B.C., Castleman, M.J., Daly, S.M., Peterson, M.M., Sully, E.K., Femling, J.K., Otto, M., Horswill, A.R., Timmins, G.S. and H.D. Gresham (2013). Nox2 modification of LDL is essential for optimal apolipoprotein B-mediated control of agr type III Staphylococcus aureus quorum-sensing. PLoS Pathogens. Feb;9(2):e1003166. doi: 10.1371/journal.ppat.1003166.

Peterson, M.M., Mack, J.L., Hall, P.R., Alsup, A.A., Alexander, S.M., Sully, E.K., Sawires, Y.S., Cheung, A.L., Otto, M. and Gresham, H.D. (2008) Apolipoprotein B is an Innate Barrier Against Invasive Staphylococcus aureus Infection. Cell Host and Microbe. 4:555-566.

Hall, P.R., Hjelle, B., Brown, D.C., Ye, C., Bondu-Hawkins, V., Kilpatrick, K.A. and Larson, R.S. (2008) Multivalent presentation of anti-hantavirus peptides on nanoparticles enhances infection blockade. Antimicrobial Agents and Chemotherapy, 52:2079-2088.

Hall P.R., Malone L, Sillerud LO, Ye C, Hjelle B and Larson RS. Characterization and NMR solution structure of a novel cyclic pentapeptide inhibitor of pathogenic hantaviruses. Chemical Biology & Drug Design, 69:180-190, 2007.

Prescott J, Hall P.R., Bondu-Hawkins V, Ye C and Hjelle B. Early Innate Immune Responses to Sin Nombre Hantavirus Occur Independently of IFN Regulatory Factor 3, Characterized Pattern Recognition Receptors, and Viral Entry. J. Immunology, 179:1796-1802, 2007.

Bell JK, Askins J, Hall P.R., Davies DR and Segal DM. The dsRNA binding site of human Toll-like receptor 3. Proc. Natl. Acad. Sci. USA 103:8792-8797, 2006.

Bell, J.K., Botos, I., Hall, P.R., Askins, J., Shiloach, J., Davies, D.R. and Segal, D.M. The molecular structure of the TLR3 extracellular domain. J Endotoxin Res. 12:375-378, 2006.

Bell JK, Botos I, Hall P.R., Askins J, Shiloach J, Segal DM, and Davies DR. The molecular structure of the Toll-like receptor 3 ligand-binding domain. Proc. Natl. Acad. Sci. USA 102:10976-10980, 2005.

Hall P.R., Zheng R, Antony L, Pusztai-Carey M, Carey PR. and Yee VC. Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit. EMBO J 23: 3621-3631, 2004.

Hall P.R., Zheng R, Pusztai-Carey M, van den Akker F, Carey PR, and Yee VC. Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit. Acta. Crystallogr. D. 60:521-523, 2004.

Hall P.R., Wang Y-F, Rivera-Hainaj RE, Zheng X, Pusztai-Carey M, Carey PR, and Yee VC. Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. EMBO J. 22:2334-2347, 2003.


The University of New Mexico’s Doctor of Pharmacy program is accredited by the Accreditation Council for Pharmacy Education, 20 North Clark Street, Suite 2500, Chicago, IL 60602-5109, TEL (312) 664-3575 , FAX (312) 664-4652, URL http://www.acpe-accredit.org/

10/29/2013 01:38:12 PM -0700.