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Blood, 1 November 2001, Vol. 98, No. 9, pp. 2657-2663
CLINICAL OBSERVATIONS, INTERVENTIONS, AND THERAPEUTIC TRIALS
A 385 insertion in the hypervariable region 1 of
hepatitis C virus E2 envelope protein is found in some patients with
mixed cryoglobulinemia type 2
Martina Gerotto,
Francesca Dal Pero,
Stefano Loffreda,
Francesco B. Bianchi,
Alfredo Alberti, and
Marco Lenzi
From the Dipartimento di Medicina Clinica e
Sperimentale, University of Padua, and the Dipartimento di Medicina
Interna, Cardioangiologia, Epatologia, Policlinico S. Orsola,
University of Bologna, Italy.
Chronic hepatitis C virus (HCV) infection has been associated with
development of mixed cryoglobulinemia type 2 (MC2), a
lymphoproliferative disorder characterized by B cell monoclonal
expansion and immunoglobulin M/k cryoprecipitable immunoglobulin
production. A short sequence (codons 384-410) of the HCV E2 protein,
which has the potential to promote B cell proliferation, was
investigated in 21 patients with HCV-related MC2 and in a control group
of 20 HCV carriers without MC2. In 6 of the 21 (29%) patients with
MC2, all the clones isolated from plasma, peripheral blood mononuclear
cells, and liver showed sequence length variation compared with the
hypervariable region 1 (HVR1) consensus sequence; 5 patients had an
insertion at codon 385, and 1 patient had a deletion at codon 384. Inserted residues at position 385 were different within and between
patients. No such mutations were observed in any of the HVR1 clones
from control patients without MC2, and the difference between the 2 groups was statistically significant (P = .02). Analysis
of 1345 HVR1 sequences obtained from GenBank strongly supported the
conclusion that the observed insertions and deletion represent a rare
event in HCV-infected patients, suggesting that they are significantly associated with MC2. The physical and chemical profiles of the 385 inserted residues detected in the MC2 patients were consistent with the
possibility that these mutations, which occurred in a region containing
immunodominant epitopes for neutralizing antibodies and binding sites
for B lymphocytes, may be selected by functional constraints for
interaction with host cells.
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