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You searched for +publisher:"Texas A&M University" +contributor:("Dickey, Burton"). Showing records 1 – 2 of 2 total matches.

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Texas A&M University

1. Francis, Mathew Prashanth. Understanding the Structural Basis for Functional Differences in Staphylococcal MSCRAMMS SDRE1 and BBP/SDRE2 and Their Role in Species Tropism.

Degree: 2015, Texas A&M University

Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) on Staphylococcus aureus play roles in attachment, invasion and immune evasion. It has been previously reported that bone sialoprotein-binding protein (Bbp) binds to human fibrinogen. Herein, we show that Bbp and SD-repeat protein E (SdrE) are allelic variants whose in vitro fibrinogen binding profile provides a rationale for the epidemiological presence of Bbp and SdrE in human and animal Staphylococcal strains. Epidemiological studies show that bbp is found in 32% of human staphylococcal strains, whereas it is nearly absent from animal staphylococcal strains. We show through basic and advanced in vitro biochemical techniques that Bbp shows a vastly higher affinity for human fibrinogen than SdrE and that Bbp specifically displays affinity for fibrinogen from humans. In contrast, SdrE shows varying affinity for fibrinogen from a wide array of various animals. The structural basis for this difference is elucidated by determining the molecular structures of Bbp and SdrE with no ligands as well as the molecular structures of Bbp and SdrE in complex with a peptide representing the fibrinogen ligand binding sequence. Data from these structural analyses were used to inform mutational analysis of the recombinant proteins, both to confirm the integrity structural models and to discover which residues are responsible for the differences in binding profile. From these data, we show that the Lock Regions of the two proteins are a major cause of this difference in binding profile and species tropism. The structural basis for this difference is elucidated by determining the molecular structures of apo-Bbp and apo-SdrE as well as the molecular structure of Bbp in complex with a peptide representing the ligand binding sequence. Data from these structural analyses were used to inform mutational analysis of the recombinant proteins, both to confirm the integrity structural models and to discover which residues are responsible for the differences in binding profile. From these data, we show that the Lock Regions of the two proteins are a major cause of this difference in binding profile and species tropism. Advisors/Committee Members: H??k, Magnus (advisor), Bondos, Sarah (committee member), Dickey, Burton (committee member), Huston, David (committee member), Xu, Yi (committee member).

Subjects/Keywords: MRSA; MSCRAMM; species tropism

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

APA (6th Edition):

Francis, M. P. (2015). Understanding the Structural Basis for Functional Differences in Staphylococcal MSCRAMMS SDRE1 and BBP/SDRE2 and Their Role in Species Tropism. (Thesis). Texas A&M University. Retrieved from http://hdl.handle.net/1969.1/155051

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Francis, Mathew Prashanth. “Understanding the Structural Basis for Functional Differences in Staphylococcal MSCRAMMS SDRE1 and BBP/SDRE2 and Their Role in Species Tropism.” 2015. Thesis, Texas A&M University. Accessed July 15, 2019. http://hdl.handle.net/1969.1/155051.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Francis, Mathew Prashanth. “Understanding the Structural Basis for Functional Differences in Staphylococcal MSCRAMMS SDRE1 and BBP/SDRE2 and Their Role in Species Tropism.” 2015. Web. 15 Jul 2019.

Vancouver:

Francis MP. Understanding the Structural Basis for Functional Differences in Staphylococcal MSCRAMMS SDRE1 and BBP/SDRE2 and Their Role in Species Tropism. [Internet] [Thesis]. Texas A&M University; 2015. [cited 2019 Jul 15]. Available from: http://hdl.handle.net/1969.1/155051.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Francis MP. Understanding the Structural Basis for Functional Differences in Staphylococcal MSCRAMMS SDRE1 and BBP/SDRE2 and Their Role in Species Tropism. [Thesis]. Texas A&M University; 2015. Available from: http://hdl.handle.net/1969.1/155051

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Texas A&M University

2. Jaramillo Hernandez, Ana Maria. Molecular and Functional Identification of Two Mucin Secretory Pathways.

Degree: PhD, Medical Sciences, 2018, Texas A&M University

In airways, secreted mucins absorb large volumes of water to form viscoelastic mucus, which is then propelled proximally by ciliary beating and swallowed. Mucins are secreted both at a low baseline rate and a high agonist-stimulated rate; baseline secretion is primarily responsible for clearance of inhaled particles and pathogens, while stimulated secretion can induce airway obstruction protectively to trap helminths traversing the lungs or pathologically in asthma. Exocytosis requires a SNARE complex acting in concert with a Munc18 scaffolding protein. We previously found that Munc18b has the major scaffolding role in stimulated mucin secretion using heterozygous knockout mice. Here, we sought to identify the Munc18 protein mediating baseline secretion, and to test the hypothesis that selective impairment of stimulated secretion can protect against airway mucus obstruction. Using conditional airway epithelial deletant mice, we found that Munc18a has the major role in baseline mucin secretion, Munc18b has the major role in stimulated mucin secretion, and Munc18c does not function in mucin secretion. In an allergic asthma model, Munc18b deletion reduced airway mucus occlusion and airflow resistance. In a cystic fibrosis model, Munc18b deletion reduced airway mucus occlusion and emphysema. Munc18b deficiency in the airway epithelium did not result in any abnormalities of lung structure, particle clearance, inflammation, or bacterial infection. Our results show that regulated secretion in a polarized epithelial cell may involve more than one exocytic machine at the apical plasma membrane, and that the protective roles of mucin secretion can be preserved while therapeutically targeting its pathologic roles. Advisors/Committee Members: Hook, Magnus (advisor), Dickey, Burton (advisor), Tuvim, Michael (committee member), Reiner, David (committee member), McNew, James (committee member), Moczygemba, Margie (committee member).

Subjects/Keywords: Munc18; mucin; exocytosis; asthma; cystic fibrosis; mucus

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

APA (6th Edition):

Jaramillo Hernandez, A. M. (2018). Molecular and Functional Identification of Two Mucin Secretory Pathways. (Doctoral Dissertation). Texas A&M University. Retrieved from http://hdl.handle.net/1969.1/174327

Chicago Manual of Style (16th Edition):

Jaramillo Hernandez, Ana Maria. “Molecular and Functional Identification of Two Mucin Secretory Pathways.” 2018. Doctoral Dissertation, Texas A&M University. Accessed July 15, 2019. http://hdl.handle.net/1969.1/174327.

MLA Handbook (7th Edition):

Jaramillo Hernandez, Ana Maria. “Molecular and Functional Identification of Two Mucin Secretory Pathways.” 2018. Web. 15 Jul 2019.

Vancouver:

Jaramillo Hernandez AM. Molecular and Functional Identification of Two Mucin Secretory Pathways. [Internet] [Doctoral dissertation]. Texas A&M University; 2018. [cited 2019 Jul 15]. Available from: http://hdl.handle.net/1969.1/174327.

Council of Science Editors:

Jaramillo Hernandez AM. Molecular and Functional Identification of Two Mucin Secretory Pathways. [Doctoral Dissertation]. Texas A&M University; 2018. Available from: http://hdl.handle.net/1969.1/174327

.