Trevor Greenhough's Outputs (24)

Crystal structures of human SP-D complexed with synthetic oligosaccharides suggest a role for phosphorylated inner core LPS saccharides in host-pathogen interactions (2025)
Preprint / Working Paper
Williams, H. M., Watson, A., Madsen, J., Clark, H. W., Hood, D. W., Oscarson, S., Greenhough, T. J., & Shrive, A. K. (2025). Crystal structures of human SP-D complexed with synthetic oligosaccharides suggest a role for phosphorylated inner core LPS saccharides in host-pathogen interactions

The innate immune protein human surfactant protein D (SP-D) recognises pathogens in the lungs via binding to carbohydrate surface structures. SP-D has been shown to target gram-negative bacterial lipopolysaccharide via calcium-dependent binding, pref... Read More about Crystal structures of human SP-D complexed with synthetic oligosaccharides suggest a role for phosphorylated inner core LPS saccharides in host-pathogen interactions.

Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs (2023)
Journal Article
Williams, H. M., Moeller, J. B., Burns, I., Schlosser, A., Sorensen, G. L., Greenhough, T. J., Holmskov, U., & Shrive, A. K. (2023). Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs. Journal of Biological Chemistry, 105552. https://doi.org/10.1016/j.jbc.2023.105552

Fibrinogen C-domain containing-1 (FIBCD1) is an immune protein proposed to be involved in host recognition of chitin on the surface of pathogens. As FIBCD1 readily binds to acetylated molecules, we have determined the high-resolution crystal structur... Read More about Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs.

Characterisation of the Structural Requirements for the Immunomodulatory Surfactant Protein D (SP-D) to Bind to Maltose Based Ligands (2022)
Journal Article
Shrive, & Greenhough. (2022). Characterisation of the Structural Requirements for the Immunomodulatory Surfactant Protein D (SP-D) to Bind to Maltose Based Ligands. https://doi.org/10.1164/ajrccm-conference.2022.205.1_MeetingAbstracts.A2609

Structural studies of C-reactive protein (2021)
Presentation / Conference Contribution
Collister, S., Neale, W., Littlejohn, J., Greenhough, T., & Shrive, A. (2021, August). Structural studies of C-reactive protein. Poster presented at XXV IUCr Congress, Prague, Czech Republic

Bacterial lipopolysaccharide recognition by surfactant protein D (2021)
Presentation / Conference Contribution
Shrive, & Greenhough. (2021, August). Bacterial lipopolysaccharide recognition by surfactant protein D. Presented at XXV IUCr Congress, Prague, Czech Republic

Human surfactant protein D is a collectin and member of the C-type lectin superfamily of proteins that forms an essential part of the mammalian innate immune system. The collectins have been recognised to not only bind to invading pathogens, allowing... Read More about Bacterial lipopolysaccharide recognition by surfactant protein D.

Lipopolysaccharide recognition by human surfactant protein D (2021)
Presentation / Conference Contribution
Neale, W., Madsen, J., Clark, H., Shrive, A., & Greenhough, T. (2021, August). Lipopolysaccharide recognition by human surfactant protein D. Poster presented at XXV IUCr Congress, Prague, Czech Republic

Structural studies of innate immune proteins (2021)
Presentation / Conference Contribution
da Silva, R., Burns, I., Greenhough, T. J., & Shrive, A. K. (2021, August). Structural studies of innate immune proteins. Poster presented at XXV IUCr Congress, Prague, Czech Republic

Structural basis of bacterial recognition by surfactant protein D (2021)
Presentation / Conference Contribution
Shrive, A., Hood, D., Clark, H., Madsen, J., & Greenhough, T. (2021, August). Structural basis of bacterial recognition by surfactant protein D. Poster presented at XXV IUCr Congress, Prague, Czech Republic

X-Ray diffraction data for structure associated with PDB ID: 6ZR4 (2020)
Data
Shrive, A., & Greenhough, T. (2020). X-Ray diffraction data for structure associated with PDB ID: 6ZR4. [Data]. https://doi.org/10.21252/2ndt-aq43

X-ray diffraction data for structure associated with PDB ID: 6ZR3 (2020)
Data
Shrive, A., & Greenhough, T. (2020). X-ray diffraction data for structure associated with PDB ID: 6ZR3. [Data]. https://doi.org/10.21252/403p-sz47

X-ray diffraction data for structure associated with PDB ID: 6ZR0 (2020)
Data
Shrive, A., & Greenhough, T. (2020). X-ray diffraction data for structure associated with PDB ID: 6ZR0. [Data]. https://doi.org/10.21252/zcfy-cw20

X-Ray diffraction data for structure associated with PDB ID: 6ZQY (2020)
Data
Shrive, A., & Greenhough, T. (2020). X-Ray diffraction data for structure associated with PDB ID: 6ZQY. [Data]. https://doi.org/10.21252/hx7e-rd04

X-ray diffraction data for structure associated with PDB ID: 6ZQX (2020)
Data
Shrive, A., & Greenhough, T. (2020). X-ray diffraction data for structure associated with PDB ID: 6ZQX. [Data]. https://doi.org/10.21252/2b3f-9369

X-ray diffraction data for structure associated with PDB ID: 6ZQR (2020)
Data
Shrive, A., & Greenhough, T. (2020). X-ray diffraction data for structure associated with PDB ID: 6ZQR. [Data]. https://doi.org/10.21252/r2nx-0425

Monomeric C-Reactive Protein in Serum With Markedly Elevated CRP Levels Shares Common Calcium-Dependent Ligand Binding Properties With an in vitro Dissociated Form of C-Reactive Protein (2020)
Journal Article
Williams, R. D., Moran, J. A., Fryer, A. A., Littlejohn, J. R., Williams, H. M., Greenhough, T. J., & Shrive, A. K. (2020). Monomeric C-Reactive Protein in Serum With Markedly Elevated CRP Levels Shares Common Calcium-Dependent Ligand Binding Properties With an in vitro Dissociated Form of C-Reactive Protein. Frontiers in Immunology, 11, Article ARTN 115. https://doi.org/10.3389/fimmu.2020.00115

A monomeric form of C-reactive protein (CRP) which precipitates with cell wall pneumococcal C polysaccharide (CWPS) and retains the ability to reversibly bind to its ligand phosphocholine has been produced through urea-induced dissociation at an opti... Read More about Monomeric C-Reactive Protein in Serum With Markedly Elevated CRP Levels Shares Common Calcium-Dependent Ligand Binding Properties With an in vitro Dissociated Form of C-Reactive Protein.

X-Ray diffraction data relating to protein structure PDB ID: 6RYG (2019)
Data
Shrive, A., & Greenhough, T. (2019). X-Ray diffraction data relating to protein structure PDB ID: 6RYG. [Data]. https://doi.org/10.21252/aram-j439

X-Ray diffraction data relating to protein structure PDB ID: 6RYM (2019)
Data
Shrive, A., & Greenhough, T. (2019). X-Ray diffraction data relating to protein structure PDB ID: 6RYM. [Data]. https://doi.org/10.21252/xbsq-d621

X-Ray diffraction data relating to protein structure PDB ID: 6RYN (2019)
Data
Shrive, A., & Greenhough, T. (2019). X-Ray diffraction data relating to protein structure PDB ID: 6RYN. [Data]. https://doi.org/10.21252/namb-4704

Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. (2019)
Journal Article
Paterson, J. M., Shaw, A. J., Burns, I., Dodds, A. W., Prasad, A., Reid, K. B., Greenhough, T. J., & Shrive, A. K. (2019). Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. Journal of biological chemistry, 294(45), 17155-17165. https://doi.org/10.1074/jbc.RA119.010271

Bovine conglutinin is an immune protein that is involved in host resistance to microbes and parasites and interacts with complement component iC3b, agglutinates erythrocytes, and neutralizes influenza A virus. Here, we determined the high-resolution... Read More about Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine..

Structural definition of hSP-D recognition of Salmonella enterica LPS inner core oligosaccharides 1 reveals alternative binding modes for the same LPS (2018)
Journal Article
Littlejohn, J. R., da Silva, R. F., Neale, W. A., Smallcombe, C. C., Clark, H. W., Mackay, R.-M. A., Watson, A. S., Madsen, J., Hood, D. W., Burns, I., Greenhough, T. J., & Shrive, A. K. (2018). Structural definition of hSP-D recognition of Salmonella enterica LPS inner core oligosaccharides 1 reveals alternative binding modes for the same LPS. PloS one, https://doi.org/10.1371/journal.pone.0199175

The crystal structures of a biologically and therapeutically active recombinant homotrimeric fragment of native human SP-D (hSP-D) complexed with the inner core oligosaccharide of the Salmonella enterica sv Minnesota rough strains R5 and R7 (rough mu... Read More about Structural definition of hSP-D recognition of Salmonella enterica LPS inner core oligosaccharides 1 reveals alternative binding modes for the same LPS.