The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab.
- J. Derrick, D. Wigley
- Biology, ChemistryJournal of Molecular Biology
- 10 November 1994
The binding site for protein G on Fab is relatively invariant across different species and gamma chain subclasses, providing an explanation for the widespread recognition of Fab fragments from mouse and human antibodies by protein G.
Characterization of two Pseudomonas putida lipopeptide biosurfactants, putisolvin I and II, which inhibit biofilm formation and break down existing biofilms
- I. Kuiper, E. Lagendijk, G. Bloemberg
- BiologyMolecular Microbiology
- 11 November 2003
Using purified putisolvin I and II it was shown that biofilm formation of different Pseudomonas strains was inhibited and most interestingly, that both putisolvins are also able to break down existing PseUDomonas biofilms.
Structure of the PilM-PilN Inner Membrane Type IV Pilus Biogenesis Complex from Thermus thermophilus
- V. Karuppiah, J. Derrick
- Biology, ChemistryJournal of Biological Chemistry
- 19 May 2011
A model in which PilM binds ATP and then PilN as one of the first steps in the formation of the inner membrane platform of the type IV pilus biogenesis complex is proposed.
Structural and Evolutionary Inference from Molecular Variation in Neisseria Porins
- J. Derrick, R. Urwin, J. Suker, I. Feavers, M. Maiden
- BiologyInfection and Immunity
- 1 May 1999
Phylogenetic analyses were consistent with an important role for horizontal genetic exchange in the emergence of different porin classes and confirmed the close evolutionary relationships of the porins from N. meningitidis, N. gonorrhoeae,Neisseria lactamica, and Neisseria polysaccharea.
Interactions between the Lipoprotein PilP and the Secretin PilQ in Neisseria meningitidis
- Seetha V. Balasingham, R. Collins, T. Tønjum
- BiologyJournal of Bacteriology
- 25 May 2007
It is found that PilP was an inner membrane protein required for pilus expression and transformation, since pilP mutants were nonpiliated and noncompetent, and this findings suggest a role for PilP in pilus biogenesis.
Structure and Assembly of a Trans-Periplasmic Channel for Type IV Pili in Neisseria meningitidis
- J. Berry, M. Phelan, J. Derrick
- BiologyPLoS Pathogens
- 1 September 2012
It is concluded that passage of the pilus fiber requires disassembly of both the membrane-spanning and the β-domain regions in PilQ, and that PilP plays an important role in stabilising the PilQ assembly during secretion, through its anchorage in the inner membrane.
Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis
- V. Karuppiah, R. Collins, A. Thistlethwaite, Ya Gao, J. Derrick
- BiologyProceedings of the National Academy of Sciences
- 11 November 2013
Three-dimensional reconstructions of the PilMNO inner membrane complex, alone and in complex with pilin protein, are reported through a combination of X-ray crystallography and electron microscopy, to provide structural information on the early events in this important secretion process.
The folic acid biosynthesis pathway in bacteria: evaluation of potential for antibacterial drug discovery.
- A. Bermingham, J. Derrick
- Biology, ChemistryBioessays
- 1 July 2002
The current knowledge of the structure and mechanism of each enzyme in the bacterial folic acid biosynthesis pathway from GTP to dihydrofolate is reviewed and conclusions regarding the potential of each enzymes as a target for therapeutic intervention are drawn.
Phylogenetic evidence for frequent positive selection and recombination in the meningococcal surface antigen PorB.
- R. Urwin, E. Holmes, A. Fox, J. Derrick, M. Maiden
- BiologyMolecular biology and evolution
- 1 October 2002
It is shown that some residues in the surface loops of PorB are under very strong positive selection, as great as that observed in human immunodeficiency virus-1 surface glycoproteins, whereas amino acids within the loops and the membrane-spanning regions of the protein are under purifying selection, presumably because of structural constraints.
Immunogenicity of therapeutic proteins: Influence of aggregation
- Kirsty D. Ratanji, J. Derrick, R. Dearman, I. Kimber
- BiologyJournal of Immunotoxicology
- 6 August 2013
An overview of the phenomenon of protein aggregation, the production of unwanted aggregates during bioprocessing, and how the immune response to aggregated protein differs from that provoked by non-aggregated protein is provided.