Journal
AIDS
Volume 19, Issue 4, Pages 381-389Publisher
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/01.aids.0000161767.21405.68
Keywords
HIV-1; pathogenesis; glycosylation; galactose-deficient IgG; Psathyrella velutina lectin; antibodies
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Funding
- NCI NIH HHS [P30 CA013148] Funding Source: Medline
- NIAID NIH HHS [AI 28147, T32 AI007051] Funding Source: Medline
- NIDCR NIH HHS [DE 13694] Funding Source: Medline
- NIDDK NIH HHS [DK 57750, DK 61525] Funding Source: Medline
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Background: The IgG from sera of patients with chronic inflammatory diseases of autoimmune character or some chronic microbial infections is frequently deficient in galactose on N-linked glycans. However, this phenomenon has not been investigated at length in human viral infections. Objectives: To evaluate the glycosylation of serum IgG in HIV-1-positive patients. Methods: Psathyrella velutina lectin was used in enzyme-linked immunosorbent and Western blot assays to determine glycosylation. In addition, gas-liquid chromatography and mass spectrometry were utilized to confirm the galactose deficiency observed in the lectin-binding assays. Results HIV-1-infected individuals had significantly higher levels of galactose-deficient IgG than healthy controls. In fact, the galactose deficiency of the N-linked glycans observed in other diseases was even more profound in HIV-1 infection. This deficiency was primarily restricted to IgG when total serum glycoproteins were evaluated and IgG1 was the subclass most affected in all patients. Also, a significant increase in lectin binding was observed on IgG2 and IgG4 from HIV-1-positive females compared with HIV-1 -negative females. Conclusions : Identification of deficient galactosylation of serum IgG from HIV-1-infected patients extended the spectrum of diseases in which this phenomenon has been observed. In addition, the results suggest yet another aspect of immune dysfunction as a result of HIV-1 infection. (c) 2005 Lippincott Williams & Wilkins.
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