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Analysis of antibody to milk proteins in HIV positive/negative sera using two-dimensional electrophoresis, western blot and immunoassay.

Abstract

Homology between the 120 envelope glycoprotein of HIV-1 virus and alpha-lactalbumin (a milk protein) stimulated interest in analysis of antibody in HIV-1 positive plasma to cow’s milk. Western blots of a two-dimensional (2-D) separation of milk were assayed with nine HIV-1 positive plasmas and nine control sera. The control sera from reference labs represented various
disease problems. All nine HIV-1 positive plasma had antibody to between two and five milk proteins. All nine HIV-1 positive plasma had antibody to albumin and immunoglobulin (IgG); in addition, seven reacted with butyrophilin, five with alpha-lactalbumin, six with casein. Four of the control sera had no antibody to milk proteins; three had minor reactivity to casein and two, one diagnosed as an IgM
Lyme positive, one diagnosed with Helicobacter pylori detected three and four milk proteins. None of the control sera had antibody to albumin or alpha-lactalbumin. Bovine and human albumin have almost identical sequence, and antibody generated to bovine serum albumin could react with human serum albumin. To look at this, three of the HIV-1 positive plasmas were assayed with 2-D Western blots of human milk and did have reactivity with albumin and IgG. Also, the protein butyrophilin is highly immunogenic and has significant homology with human neural and cellular proteins. Whether these antibodies can be causing allergy or autoimmune
disease is speculative, but they indicate an immune system which is highly activated.

Proteomics. 2001 May;1(5):721-5. [1]