-transparent.png){kind=logo}
Complement-mediated lysis of reconstituted lipid-myelin basic protein (BP) vesicles and myelin vesicles due to antibody raised against BP and isolated myelin is measured by determination of the amount of a water-soluble spin label, tempocholine chloride, released from the vesicles. The response is shown to be antigen-specific, antibody-dependent, and complement mediated. The relative response to different anti-BP antibody samples is similar to that determined by radioimmunoassay procedures. In contrast to immunoassays with BP in aqueous solution, this method measures immune recognition of the protein in either a synthetic or a natural membranous environment. This is important because this protein has been shown to have a different conformation when bound to lipid bilayers than in aqueous solution and its conformation depends on lipid composition. It is also a more rapid method because no separation of spin label still trapped in the vesicles and that released due to immune lysis is required. In synthetic membranes consisting of sphingomyelin, cholesterol, and an acidic lipid, either phosphatidylglycerol, phosphatidic acid, or phosphatidylserine, the response was greatest when the acidic lipid was phosphatidic acid. The response did not depend significantly on the antigen concentration expressed as molar ratio of BP to sphingomyelin, over the range 0.15:600 to 2:600, although it decreased at molar ratios less than 0.15:600. The antigen density required for immune lysis of vesicles containing this protein antigen is similar to that reported elsewhere for lipid antigens, although the time required for maximal lysis was greater. Both anti-BP and anti-myelin antibodies caused a greater specific complement-mediated response with synthetic vesicles than with myelin vesicles, which may be due to the different lipid and/or protein composition of myelin. Response was also obtained with the myelin vesicles, however, indicating that some determinants of BP can be recognized on the surface of the bilayer in isolated myelin by anti-BP.
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
December 2007,
Biochimica et biophysica acta,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
October 1995,
Biochemistry,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
October 1974,
The Biochemical journal,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
September 1985,
Journal of neurochemistry,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
October 2023,
Biochimica et biophysica acta. Biomembranes,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
December 1976,
Biochimica et biophysica acta,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
January 2000,
Biochimica et biophysica acta,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
August 1999,
Journal of neuroscience research,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
April 1997,
Biochemistry,
J M Boggs, and
N Samji, and
M A Moscarello, and
G A Hashim, and
E D Day
August 1987,
Bollettino della Societa italiana di biologia sperimentale,
