1. Sialic acid-binding protein Sp2CBMTD protects mice against lethal challenge with emerging influenza A (H7N9) virus.

    Antimicrobial Agents and Chemotherapy 59(3):1495 (2015) PMID 25534734 PMCID PMC4325779

    Compounds that target the cellular factors essential for influenza virus replication represent an innovative approach to antiviral therapy. Sp2CBMTD is a genetically engineered multivalent protein that masks sialic acid-containing cellular receptors on the respiratory epithelium, which are recog...
  2. Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factor.

    BMC Structural Biology 15(1):15 (2015) PMID 26289431 PMCID PMC4546082

    Streptococcus pneumoniae Neuraminidase A (NanA) is a multi-domain protein anchored to the bacterial surface. Upstream of the catalytic domain of NanA is a domain that conforms to the sialic acid-recognising CBM40 family of the CAZY (carbohydrate-active enzymes) database. This domain has been ide...
  3. Erratum to: Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factor.

    BMC Structural Biology 15(1):19 (2015) PMID 26444866 PMCID PMC4596311

  4. Prevention of influenza by targeting host receptors using engineered proteins.

    PNAS 111(17):6401 (2014) PMID 24733924

    There is a need for new approaches for the control of influenza given the burden caused by annual seasonal outbreaks, the emergence of viruses with pandemic potential, and the development of resistance to current antiviral drugs. We show that multivalent biologics, engineered using carbohydrate-b...
  5. Enhancing the receptor affinity of the sialic acid-binding domain of Vibrio cholerae sialidase through multivalency.

    Journal of Biological Chemistry 284(11):7339 (2009) PMID 19124471 PMCID PMC2652270

    Many glycoside hydrolases possess carbohydrate-binding modules (CBMs) that help target these enzymes to appropriate substrates and increase their catalytic efficiency. The Vibrio cholerae sialidase contains two CBMs, one of which is designated as a family CBM40 module and has been shown through ...
  6. The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus.

    Journal of Biological Chemistry 279(42):43886 (2004) PMID 15265860

    The hyperthermophilic Archaea Sulfolobus solfataricus grows optimally above 80 degrees C and metabolizes glucose by a non-phosphorylative variant of the Entner-Doudoroff pathway. In this pathway glucose dehydrogenase and gluconate dehydratase catalyze the oxidation of glucose to gluconate and th...
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  7. Sialic acid recognition by Vibrio cholerae neuraminidase.

    Journal of Biological Chemistry 279(39):40819 (2004) PMID 15226294

    Vibrio cholerae neuraminidase (VCNA) plays a significant role in the pathogenesis of cholera by removing sialic acid from higher order gangliosides to unmask GM1, the receptor for cholera toxin. We previously showed that the structure of VCNA is composed of a central beta-propeller catalytic dom...
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  8. Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile.

    European Journal of Biochemistry 269(24):6250 (2002) PMID 12473121

    The crystal structure of citrate synthase from the thermophilic Archaeon Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has been determined, extending the number of crystal structures of citrate synthase from different organisms to a total of five that span the temperature r...
  9. Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion.

    Journal of Virology 76(4):1816 (2002) PMID 11799177 PMCID PMC135884

    We recently reported the first crystal structure of a paramyxovirus hemagglutinin-neuraminidase (HN) from Newcastle disease virus. This multifunctional protein is responsible for binding to cellular sialyl-glycoconjugate receptors, promotion of fusion through interaction with the second viral su...