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You searched for +publisher:"University of New Mexico" +contributor:("Gresham, Hattie"). Showing records 1 – 3 of 3 total matches.

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University of New Mexico

1. Sully, Erin. Small molecule inhibition of Staphylococcus aureus virulence.

Degree: Biomedical Sciences Graduate Program, 2011, University of New Mexico

The increasing emergence of antibiotic resistant Staphylococcus aureus infections, particularly those caused by a single clone of methicillin resistant S. aureus (USA300 MRSA), coupled with the slowing of antibiotic discovery makes research into novel therapies a priority (Lowy, 2007). One strategy evolving is the development of drugs that target bacterial virulence factors as opposed to growth (Cegelski et al., 2008). Due to the lack of selective pressure, bacterial resistance to the drugs would be minimized while the infection, attenuated by the inhibition of virulence factor production, could be cleared by the innate immune factors of the host. Virulence factors identified to date as essential for invasive USA 300 MRSA infection are globally regulated in part by a quorum sensing operon, agr (George and Muir, 2007; Novick and Geisinger, 2008; Yarwood and Schlievert, 2003). Host factors like apolipoprotein B provide defense by antagonizing agr signaling which demonstrates that host defense against an invasive infection could be accomplished by blocking agr signaling (Peterson et al., 2008). Therefore, we hypothesized that screening small molecule inhibitors for inhibition of agr signaling could contribute to drug discovery by providing optimal host defense against quorum sensing dependent S. aureus infections. Our work focuses on two small molecule inhibitors, CID# 2333 and CID# 3243271, identified in a screen of over 20,000 compounds for antagonism of agr signaling. These compounds demonstrate virulence factor inhibition in vitro and in an in vivo model of community associated -MRSA dermonecrotic infection. Advisors/Committee Members: Gresham, Hattie, Gresham, Hattie, Hall, Pamela, Mold, Carolyn, Ozbun, Michelle.

Subjects/Keywords: CA-MRSA; staphylococcus aureus; small molecule inhibitor; high-throughput screen; virulence; quorum sensing

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Sully, E. (2011). Small molecule inhibition of Staphylococcus aureus virulence. (Doctoral Dissertation). University of New Mexico. Retrieved from https://digitalrepository.unm.edu/biom_etds/39

Chicago Manual of Style (16th Edition):

Sully, Erin. “Small molecule inhibition of Staphylococcus aureus virulence.” 2011. Doctoral Dissertation, University of New Mexico. Accessed July 21, 2019. https://digitalrepository.unm.edu/biom_etds/39.

MLA Handbook (7th Edition):

Sully, Erin. “Small molecule inhibition of Staphylococcus aureus virulence.” 2011. Web. 21 Jul 2019.

Vancouver:

Sully E. Small molecule inhibition of Staphylococcus aureus virulence. [Internet] [Doctoral dissertation]. University of New Mexico; 2011. [cited 2019 Jul 21]. Available from: https://digitalrepository.unm.edu/biom_etds/39.

Council of Science Editors:

Sully E. Small molecule inhibition of Staphylococcus aureus virulence. [Doctoral Dissertation]. University of New Mexico; 2011. Available from: https://digitalrepository.unm.edu/biom_etds/39


University of New Mexico

2. Marjon, Kristopher. Immune regulation and Fc(alpha)RI Recognition and activation by C-reactive protein.

Degree: Biomedical Sciences Graduate Program, 2012, University of New Mexico

The acute phase serum protein C-reactive protein (CRP) is one of the major responding proteins during inflammation response in humans. CRP is a serum pattern recognition molecule that can bind to dead or damaged cells and bacteria to initiate their clearance through interaction with immunoglobulin receptors expressed on the surface of immune cells. Immunoglobulin receptors are traditionally thought to bind exclusively to the fragment crystallizable (Fc) region of immunoglobulins and are consequently called Fc receptors (FcRs). FcRs have been shown to play an immunoregulatory role by either exacerbating inflammatory states or potently inhibiting or reversing inflammation. CRP has been proposed to act through FcRs either promoting inflammation or resolving an inflammatory insult. Immunosuppressive properties have been demonstrated for CRP in mouse models of immune complex mediated inflammation and autoimmune disease. However, the initiating and downstream mechanisms of this process have not been investigated. This dissertation uses an adoptive cell transfer model in mice to address the immunosuppressive capacity of CRP. In this model, treatment of donor spleen cells with CRP suppresses the induced platelet clearance in recipient mice and indicates that protection by CRP is dependent on expression of FcγRI on donor macrophages and FcγRIIb in the recipient mouse. As an extension of the work characterizing CRP-FcR interactions, this dissertation also describes the IgA Fc receptor I (FcαRI) as a novel receptor for CRP. The interaction between CRP and FcαRI induces cytokine production, enhances phagocytosis and alters surface expression of FcαRI on human neutrophils. Collectively, these findings highlight key components in CRP-mediated immunosuppression and a novel receptor for CRP, indicating the complex role this ancient molecule has in the human immune system. Advisors/Committee Members: Du Clos, Terry, Mold, Carolyn, Prossnitz, Eric, Gresham, Hattie.

Subjects/Keywords: C-REACTIVE PROTEIN; MACROPHAGE; CD89; Fc alpha RI; CD64

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Marjon, K. (2012). Immune regulation and Fc(alpha)RI Recognition and activation by C-reactive protein. (Doctoral Dissertation). University of New Mexico. Retrieved from https://digitalrepository.unm.edu/biom_etds/54

Chicago Manual of Style (16th Edition):

Marjon, Kristopher. “Immune regulation and Fc(alpha)RI Recognition and activation by C-reactive protein.” 2012. Doctoral Dissertation, University of New Mexico. Accessed July 21, 2019. https://digitalrepository.unm.edu/biom_etds/54.

MLA Handbook (7th Edition):

Marjon, Kristopher. “Immune regulation and Fc(alpha)RI Recognition and activation by C-reactive protein.” 2012. Web. 21 Jul 2019.

Vancouver:

Marjon K. Immune regulation and Fc(alpha)RI Recognition and activation by C-reactive protein. [Internet] [Doctoral dissertation]. University of New Mexico; 2012. [cited 2019 Jul 21]. Available from: https://digitalrepository.unm.edu/biom_etds/54.

Council of Science Editors:

Marjon K. Immune regulation and Fc(alpha)RI Recognition and activation by C-reactive protein. [Doctoral Dissertation]. University of New Mexico; 2012. Available from: https://digitalrepository.unm.edu/biom_etds/54


University of New Mexico

3. Peterson, Meghan Michal. Apolipoprotein B-mediated control of Staphylococcus aureus virulence.

Degree: Biomedical Sciences Graduate Program, 2010, University of New Mexico

Staphylococcus aureus is a colonizer of the human skin and mucosa that can cause minor to severe disease. Originally afflicting patients at the extremes of age or those with immunocompromising co-morbidities, S. aureus strains have emerged that cause invasive disease in otherwise healthy populations with no health-care associated risk factors. In addition, these community-acquired strains predominately contain antibiotic resistance genes, making them difficult to treat with conventional interventions. Invasive disease in S. aureus is partly regulated by a quorum sensing signaling system that relies on the secretion and signaling function of a bacterial peptide pheromone (AIP). S. aureus strains that lack this virulence regulator system still cause disease, but it is much less severe and is typified by a colonizing, rather than an invasive, phenotype. Therapeutics or host factors that inhibit virulence instead of viability can limit both invasive disease as well as the development of resistance. During infection, the inflammatory process causes serum to extravasate into the affected tissue site. Serum has been shown to inhibit virulence signaling in S. aureus, though the mechanism is unknown. This dissertation identifies apolipoprotein B (apoB), the major protein component of very low and low density lipoproteins, as a potent inhibitor of virulence signaling in S. aureus by binding the bacterial signaling pheromone AIP. Though binding of host lipoproteins to bacterial products has been described in Gram-negative infections, this is the first demonstration of a lipoprotein component having protective effects in a Gram-positive infection. This work further describes the inhibitory action of apoB on virulence signaling and subsequent invasive infection in multiple S. aureus strains and identifies the globular amino terminal domain of apoB as the AIP binding site. These findings have important implications for understanding the host-pathogen interaction and for developing therapeutics that can be effective without causing bacterial resistance. Advisors/Committee Members: Gresham, Hattie, Mold, Carolyn, Chackerian, Bryce, Timmins, Graham, Hall, Pamela.

Subjects/Keywords: MRSA; S. aureus; host defense; serum lipoproteins; apolipoprotein B; infection

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Peterson, M. M. (2010). Apolipoprotein B-mediated control of Staphylococcus aureus virulence. (Doctoral Dissertation). University of New Mexico. Retrieved from https://digitalrepository.unm.edu/biom_etds/16

Chicago Manual of Style (16th Edition):

Peterson, Meghan Michal. “Apolipoprotein B-mediated control of Staphylococcus aureus virulence.” 2010. Doctoral Dissertation, University of New Mexico. Accessed July 21, 2019. https://digitalrepository.unm.edu/biom_etds/16.

MLA Handbook (7th Edition):

Peterson, Meghan Michal. “Apolipoprotein B-mediated control of Staphylococcus aureus virulence.” 2010. Web. 21 Jul 2019.

Vancouver:

Peterson MM. Apolipoprotein B-mediated control of Staphylococcus aureus virulence. [Internet] [Doctoral dissertation]. University of New Mexico; 2010. [cited 2019 Jul 21]. Available from: https://digitalrepository.unm.edu/biom_etds/16.

Council of Science Editors:

Peterson MM. Apolipoprotein B-mediated control of Staphylococcus aureus virulence. [Doctoral Dissertation]. University of New Mexico; 2010. Available from: https://digitalrepository.unm.edu/biom_etds/16

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