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Magnus Höök

Höök, Magnus
Magnus Höök
Professor of Biochemistry and Biophysics, of the IBT-Houston, and of Veterinary Anatomy and Public Health Director, Center for Extracellular Matrix Biology
Email:
Phone:
713-677-7716
Undergraduate Education
B.S. University of Uppsala, Sweden (1971)
Graduate Education
Ph.D. University of Uppsala, Sweden (1974)
Joined Texas A&M in 1992

Microbial Pathogenesis / Virulence Factors / Cell Adhesion

The primary interest of our laboratory is to try to understand the structural function of the extracellular matrix. Of particular interest is the study of the molecular mechanisms of microbial adhesion to host tissue. This process, which is believed to represent a critical initial step in the development of infections, involves specific cell-surface proteins that recognize and bind with a high affinity to components in the host tissue. Our goal is to decipher these events at a molecular level and, based on structural analysis of the interacting components, design new strategies to prevent and treat infections.

Recent Publications

  1. Casillas-Ituarte, NN, Cruz, CHB, Lins, RD, DiBartola, AC, Howard, J, Liang, X et al.. Amino acid polymorphisms in the fibronectin-binding repeats of fibronectin-binding protein A affect bond strength and fibronectin conformation. J. Biol. Chem. 2017;292 (21):8797-8810.
    doi: 10.1074/jbc.M117.786012. PubMed PMID:28400484. PubMed Central PMC5448106.

  2. Munoz-Pinto, DJ, Erndt-Marino, JD, Becerra-Bayona, SM, Guiza-Arguello, VR, Samavedi, S, Malmut, S et al.. Evaluation of late outgrowth endothelial progenitor cell and umbilical vein endothelial cell responses to thromboresistant collagen-mimetic hydrogels. J Biomed Mater Res A. 2017;105 (6):1712-1724.
    doi: 10.1002/jbm.a.36045. PubMed PMID:28218444. .

  3. Ganesh, VK, Liang, X, Geoghegan, JA, Cohen, AL, Venugopalan, N, Foster, TJ et al.. Lessons from the Crystal Structure of the S. aureus Surface Protein Clumping Factor A in Complex With Tefibazumab, an Inhibiting Monoclonal Antibody. EBioMedicine. 2016;13 :328-338.
    doi: 10.1016/j.ebiom.2016.09.027. PubMed PMID:27789272. PubMed Central PMC5264652.

  4. Liang, X, Garcia, BL, Visai, L, Prabhakaran, S, Meenan, NA, Potts, JR et al.. Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs. PLoS ONE. 2016;11 (7):e0159118.
    doi: 10.1371/journal.pone.0159118. PubMed PMID:27434228. PubMed Central PMC4951027.

  5. Arora, S, Uhlemann, AC, Lowy, FD, Hook, M. A Novel MSCRAMM Subfamily in Coagulase Negative Staphylococcal Species. Front Microbiol. 2016;7 :540.
    doi: 10.3389/fmicb.2016.00540. PubMed PMID:27199900. PubMed Central PMC4850167.

  6. Garcia, BL, Zhi, H, Wager, B, Höök, M, Skare, JT. Borrelia burgdorferi BBK32 Inhibits the Classical Pathway by Blocking Activation of the C1 Complement Complex. PLoS Pathog. 2016;12 (1):e1005404.
    doi: 10.1371/journal.ppat.1005404. PubMed PMID:26808924. PubMed Central PMC4725857.

  7. Ko, YP, Kang, M, Ganesh, VK, Ravirajan, D, Li, B, Höök, M et al.. Coagulase and Efb of Staphylococcus aureus Have a Common Fibrinogen Binding Motif. MBio. 2016;7 (1):e01885-15.
    doi: 10.1128/mBio.01885-15. PubMed PMID:26733070. PubMed Central PMC4725008.

  8. Somarajan, SR, La Rosa, SL, Singh, KV, Roh, JH, Höök, M, Murray, BE et al.. The fibronectin-binding protein Fnm contributes to adherence to extracellular matrix components and virulence of Enterococcus faecium. Infect. Immun. 2015;83 (12):4653-61.
    doi: 10.1128/IAI.00885-15. PubMed PMID:26371130. PubMed Central PMC4645382.

  9. Cereceres, S, Touchet, T, Browning, MB, Smith, C, Rivera, J, Höök, M et al.. Chronic Wound Dressings Based on Collagen-Mimetic Proteins. Adv Wound Care (New Rochelle). 2015;4 (8):444-456.
    doi: 10.1089/wound.2014.0614. PubMed PMID:26244101. PubMed Central PMC4505774.

  10. Prasad, JM, Gorkun, OV, Raghu, H, Thornton, S, Mullins, ES, Palumbo, JS et al.. Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense. Blood. 2015;126 (17):2047-58.
    doi: 10.1182/blood-2015-04-639849. PubMed PMID:26228483. PubMed Central PMC4616238.

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