Receptor Binding Sites and Antigenic Epitopes on the Fiber Knob of Human Adenovirus Serotype 3

ABSTRACT The adenovirus fiber knob causes the first step in the interaction of adenovirus with cell membrane receptors. To obtain information on the receptor binding site(s), the interaction of labeled cell membrane proteins to synthetic peptides covering the adenovirus type 3 (Ad3) fiber knob was studied. Peptide P6 (amino acids [aa] 187 to 200), to a lesser extent P14 (aa 281 to 294), and probably P11 (aa 244 to 256) interacted specifically with cell membrane proteins, indicating that these peptides present cell receptor binding sites. Peptides P6, P11, and P14 span the D, G, and I β-strands of the R-sheet, respectively. The other reactive peptides, P2 (aa 142 to 156), P3 (aa 153 to 167), and P16 (aa 300 to 319), probably do not present real receptor binding sites. The binding to these six peptides was inhibited by Ad3 virion and was independent of divalent cations. We have also screened the antigenic epitopes on the knob with recombinant Ad3 fiber, recombinant Ad3 fiber knob, and Ad3 virion-specific antisera by enzyme-linked immunosorbent assay. The main antigenic epitopes were presented by P3, P6, P12 (aa 254 to 269), P14, and especially the C-terminal P16. Peptides P14 and P16 of the Ad3 fiber knob were able to inhibit Ad3 infection of cells.

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Diffusion of target cell membrane proteins allows recognition of cryptic binding sites by Mycoplasma pulmonis hemagglutinin.

Infection and Immunity ◽

10.1128/iai.48.2.579-580.1985 ◽

1985 ◽

Vol 48 (2) ◽

pp. 579-580

Author(s):

F C Minion ◽

J D Goguen

Keyword(s):

Membrane Proteins ◽

Cell Membrane ◽

Target Cell ◽

Binding Sites ◽

Mycoplasma Pulmonis ◽

Cell Membrane Proteins ◽

Target Cell Membrane ◽

Cryptic Binding Sites

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Cyclic Adenosine Monophosphate-dependent Phosphorylation of Specific Fat Cell Membrane Proteins by an Endogenous Membrane-bound Protein Kinase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)42137-6 ◽

1974 ◽

Vol 249 (21) ◽

pp. 6854-6865 ◽

Cited By ~ 7

Author(s):

Kwen-Jen Chang ◽

Norman A. Marcus ◽

Pedro Cuatrecasas

Keyword(s):

Protein Kinase ◽

Membrane Proteins ◽

Cell Membrane ◽

Cyclic Adenosine Monophosphate ◽

Adenosine Monophosphate ◽

Fat Cell ◽

Cell Membrane Proteins ◽

Membrane Bound

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Novel autoantibodies against muscle-cell membrane proteins in patients with myositis

Arthritis & Rheumatism ◽

10.1002/art.1780391112 ◽

1996 ◽

Vol 39 (11) ◽

pp. 1860-1868 ◽

Cited By ~ 9

Author(s):

Bruno Stuhlmüller ◽

Ricardo Jerez ◽

Gert Hausdorf ◽

Hans-R. Barthel ◽

Michael Meurer ◽

...

Keyword(s):

Membrane Proteins ◽

Cell Membrane ◽

Muscle Cell ◽

Cell Membrane Proteins ◽

Muscle Cell Membrane

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Identification of novel therapeutic targets for histone 3 mutated children’s brain tumour, using unique tumour cell surface proteomic signatures

Neuro-Oncology ◽

10.1093/neuonc/noab195.019 ◽

2021 ◽

Vol 23 (Supplement_4) ◽

pp. iv9-iv9

Author(s):

Anya Snary ◽

Richard Grundy ◽

Rob Layfield ◽

Ruman Rahman ◽

Farhana Haque

Keyword(s):

Membrane Proteins ◽

Cell Membrane ◽

Cell Surface ◽

Brain Tumours ◽

Expression Patterns ◽

Surface Membrane ◽

Therapeutic Targets ◽

Molecular Signature ◽

Histone 3 ◽

Cell Membrane Proteins

Abstract Aims Improvements in the treatments for childhood and adolescent brain tumours, High-Grade Glioma (pHGG) and Diffuse Intrinsic Pontine Glioblastoma (DIPG), have not advanced much and they continue to carry a very poor prognosis. These brain tumours are now defined by mutations affecting histone 3 proteins, indeed 80% of DIPGs harbour histone H3.1 and H3.3 K27M somatic mutations whilst 30% of pHGGs exhibit H3.3 G34R or G34V mutations. We hypothesized that the histone 3 mutant tumours will have distinct mutation specific surfactome (cell membrane proteins) signature. Method We therefore analysed the cell surface proteomics of pHGG and DIPG, in order to identify novel targets for therapy. We have at first isolated the cell membrane fractions from a range of patient cells carrying different histone 3 mutations (G34R, G34V), relative to wild type histone 3. A comparative quantitative mass-spectrometry analyses of these cell surface membrane fractions is then performed. Results The results obtained to date demonstrated unique differential cell membrane expression patterns which correlated to specific mutation type. For example, increased expression of Ras-related proteins Rab-3, Rab-3D is detected only in histone H3.3-G34R mutated cell line in comparison. Conclusion Identification and analyses of these unique cell membrane proteins’ association with specific in H3.3 mutation in pHGG, will help to identify precise mutation specific therapeutic targets, benefiting the patients to receive therapy based on tumour’s molecular signature.

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