Molecular biology of the hepatitis C viruses: Implications for diagnosis, development and control of viral disease

Houghton, Michael; Weiner, Amy J.; Han, Jang H.; Kuo, George; Choo, Qui‐Lim

doi:10.1002/hep.1840140227

Cited by 806 publications

(379 citation statements)

References 57 publications

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“…F(abЈ) 2 were obtained by proteolytic cleavage of the IgG by pepsin. Briefly, the purified IgG were mixed with pepsin-agarose in an acidic buffer and digested for 1.5 h at 37°C.…”

Section: Ab Fragment Generationmentioning

confidence: 99%

“…Briefly, the purified IgG were mixed with pepsin-agarose in an acidic buffer and digested for 1.5 h at 37°C. The pepsin-agarose was then eliminated by centrifugation, and F(abЈ) 2 were recovered in the supernatant. F(abЈ) 2 were further purified by size exclusion chromatography on a Superdex 200 column (Pharmacia Biotech).…”

Section: Ab Fragment Generationmentioning

confidence: 99%

“…FabЈ were obtained by reducing with 2-ME the most labile disulfide bridges of F(abЈ) 2 and by blocking the corresponding free cysteine residue with iodoacetamide. FabЈ were further purified by size exclusion chromatography on a Superdex 200 column (Pharmacia Biotech).…”

Section: Ab Fragment Generationmentioning

confidence: 99%

“…Among the structural proteins, the core protein is derived from the amino terminus of the viral polypeptide (aa , and it is thought to form the nucleocapsid of the virion, as its sequence and biological properties resemble those of nucleocapsid proteins from other viruses. The core Ag is highly conserved among the various HCV genotypes (2) and elicits a rapid Ab response after the onset of the disease. Thus, the measurement of HCV core Ab titer in serum is widely used to screen for HCV infection (3).…”

mentioning

confidence: 99%

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Crystal Structure of a Hydrophobic Immunodominant Antigenic Site on Hepatitis C Virus Core Protein Complexed to Monoclonal Antibody 19D9D6

Ménez

Bossus

Müller

et al. 2003

The Journal of Immunology

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The first crystal structure of a complex between a hepatitis C virus (HCV) core protein-derived peptide (residues 13–40) and the Ab fragment of a murine mAb (19D9D6) has been solved, allowing determination of the recognized epitope and elucidation of its conformation. This Ab, raised against the first 120 residues of the core protein, recognizes core particles and strongly competes with anticore human Abs, suggesting that it is highly representative of the human anti-HCV core response. Its epitope lies within the first 45 aa of the protein, the major antigenic segment of core recognized both by murine and human Abs. Surprisingly, the recognized epitope (29–37: QIVGGVYLL) has an unusual preponderance of hydrophobic residues, some of which are buried in a small hydrophobic core in the nuclear magnetic resonance structure of the peptide (2–45) in solution, suggesting that the Ab may induce a structural rearrangement upon recognition. The flexibility may reside entirely within the Ag, since the Fab′-peptide complex structure at 2.34 Å shows that the Ab binding site is hardly perturbed by complexation. Given that the recognized residues are unlikely to be solvent exposed, we are left with the interesting possibility that Ab-core interactions may take place in a nonaqueous environment.

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“…F(abЈ) 2 were obtained by proteolytic cleavage of the IgG by pepsin. Briefly, the purified IgG were mixed with pepsin-agarose in an acidic buffer and digested for 1.5 h at 37°C.…”

Section: Ab Fragment Generationmentioning

confidence: 99%

Section: Ab Fragment Generationmentioning

confidence: 99%

Section: Ab Fragment Generationmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Crystal Structure of a Hydrophobic Immunodominant Antigenic Site on Hepatitis C Virus Core Protein Complexed to Monoclonal Antibody 19D9D6

Ménez

Bossus

Müller

et al. 2003

The Journal of Immunology

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“…Possible variables include localised corneal factors, requirement of antigen antibody ratios in the serum within a specific range to yield immune complexes of an appropriate size to deposit in the cornea from the limbal vessels, genetic immune response difference between individuals infected with HCV, and the well-documented diversity of HCV. 31 Hepatitis C also is a flavivirus that can be detected with available antibody tests. But four new hepatitis viruses have been discovered.…”

Section: Discussionmentioning

confidence: 99%

Hepatitis C virus-associated keratitis

Jain

Sukhija

Saini

et al. 2004

Eye

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Aim To study the association between chronic hepatitis C virus (HCV) and Mooren's type keratitis. Method A total of 50 patients with chronic HCV were screened for any evidence of corneal ulceration. Detailed ocular examination was conducted by slit-lamp biomicroscopy. Patients with history of trauma to the eye or previous herpetic keratitis were excluded from the study. Results There were 37 males and 13 females.

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Hepatitis C Virus in Dermatology

Pawlotsky¹

1995

Arch Dermatol

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Molecular biology of the hepatitis C viruses: Implications for diagnosis, development and control of viral disease

Cited by 806 publications

References 57 publications

Crystal Structure of a Hydrophobic Immunodominant Antigenic Site on Hepatitis C Virus Core Protein Complexed to Monoclonal Antibody 19D9D6

Crystal Structure of a Hydrophobic Immunodominant Antigenic Site on Hepatitis C Virus Core Protein Complexed to Monoclonal Antibody 19D9D6

Hepatitis C virus-associated keratitis

Hepatitis C Virus in Dermatology

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