THE MAJOR SITE OF GUINEA‐PIG MYELIN BASIC PROTEIN ENCEPHALITOGENIC IN LEWIS RATS<sup>1</sup><sup>2</sup>

Chou, C H; Chou, Frank C.‐H.; Kowalski, Thomas J.; Shapira, Raymond; Kibler, Robert F.

doi:10.1111/j.1471-4159.1977.tb07716.x

Cited by 109 publications

(46 citation statements)

References 15 publications

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“…to exhibit a diverse conformational variability both in solution (Eylar & Thompson, 1969;Chao & Einstein, 1970;Palmer & Dawson, 1969;Liebes et al, 1975;Stone et al, 1985;Mendz et al, 1984) and when bound to lipids (Surewicz et al, 1987;Keniry & Smith, 1979).…”

mentioning

confidence: 99%

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Pj²,

Marsh

1989

Biochemistry

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The myelin basic protein (MBP) from bovine spinal cord was cleaved at the single tryptophan residue to produce an N-terminal fragment ( F l ) of molecular weight 12.6K and a C-terminal fragment (F2) of molecular weight 5.8K. The interactions of the two fragments with bilayers of the acidic lipid dimyristoylphosphatidylglycerol (DMPG) were compared with those of the intact protein, by using both chemical binding assays and spin-label electron spin resonance spectroscopy. The saturation binding stoichiometries of the two fragments were found to sum to that of the MBP, having values of 1 1, 24, and 36 mol of DMPG/mol of protein for F2, F1, and the MBP, respectively. The strength of binding was found to increase in the order F2 < F1 < MBP, which follows that of the net charges on the different fragments.The ionic strength dependence of the protein binding indicated that the interaction is primarily of electrostatic origin. The efficiency of displacement of the proteins by salt was in the order F2 > F1 > MBP, which correlates with both the strength of binding and the net charge on the different protein fragments. Nitroxide derivatives of phosphatidylglycerol (PG) labeled on the sn-2 chain were used to probe the protein-induced changes in the acyl chain dynamics. Both the fragments and the MBP decreased the lipid chain mobility as recorded by the C-5 atom and (2-12 atom position nitroxide-PG spin-labels, in a manner which followed the protein binding curves. At saturation binding, the reduction in mobility recorded by the C-5 atom label was in the order M B P > F1 > F2. An additional population of lipids, whose chain motion was restricted relative to that of the bulk population of fluid lipids, was resolved in the case of the F1 fragment and the MBP, when using the C-12 atom position labeled PG. Approximately nine DMPG molecules per F1 fragment were found in this motionally restricted population, which was assigned to lipids in direct contact with partially penetrant sections of the protein, as opposed to a 18: 1 mol/mol lipid/protein stoichiometry found for the restricted component with the intact MBP. These results suggest that the principal sites of hydrophobic interaction of the protein with lipid bilayers are at least partly located in the 12.6-kDa fragment. The tryptophan residue at position 116 appears also to be important for the structural and functional properties of the intact bovine myelin basic protein.x e water-soluble peripheral myelin basic protein (MBP)' plays an important role in the structural organization of the myelin sheath [see Boggs and Moscarello (1978a,b) and Boggs et al. (1982)l. Induction and maintenance of the multilamellar structure of myelin are thought to be brought about by a bridging of apposing cytoplasmic surfaces. A hairpin structure of the protein caused by a tri-proline sequence approximately in the middle of the molecule is considered to cause interlamellar interactions (Eylar et al., 1971).

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confidence: 99%

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Pj²,

Marsh

1989

Biochemistry

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“…These features of parahel properties, that can be related to homologies in peptide sequences, may also be reflected in the antigenic properties of the cholera toxin homologous peptides. In human MBP the sequence from residue 43 to 88 is a dominant antigenic form present in cerebrospinal fluid after myelin injury 1181 and contains the major encephalitogenic determinant reported to be responsible for EAE in Lewis rat [19], rabbit [20] and monkey [21]. This sequence contains the epitope residues 64-75 [22], which are part of the MBP sequence 67-77 that in turn is homologous to the chol A segment of amino acids 130 to 140.…”

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confidence: 99%

Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

Caamaño¹,

Zand²

1989

FEBS Letters

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Recent reports that myelin basic protein (MBP) can be ADP-ribosylated and contains specific sites that bind GTP and Gu, ganglioside, have suggested an analogy to the properties of cholera toxin. Comparisons of pairs of sequences between these two proteins yielded two regions of homology between MBP and the cholera toxin B (chol B) subunit, and one region of homology with the cholera toxin A (chol A) subunit. The matching sites within chol B consisted of a 17 amino acid residue sequence (residues 3046 in chol B and residues 102-I 18 in human-MBP, hMBP, p < 0.0007) and an 11 residue span (residues 3141 in chol B and sequence 29-39 in hMBP, p

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“…Peptide 79-88 was prepared by tryptic digestion of the guinea pig peptide 43-88 pretreated with citraconic anhydride followed by regeneration in dilute acid. The peptide was isolated on CM-cellulose and further purified on Sephadex G25 (14). The guinea pig peptide 43-88 was used instead of the corresponding bovine peptide since it is not possible to obtain peptide 79-88 from the bovine peptide 43-88 because of a resistant Arg-Pro peptide bond at position 78-79.…”

Section: Fragmentation Of Bp (Component 1)mentioning

confidence: 99%

“…Bovine peptide 43-88 was subjected to limited chymotrypsin digestion (protein to enzyme ratio, 1,000:1) to produce peptides 43-67 (C2) and 68-88 (C1) which were separated on CM-cellulose and further purified on Sephadex GS0 (14). Peptide 79-88 was prepared by tryptic digestion of the guinea pig peptide 43-88 pretreated with citraconic anhydride followed by regeneration in dilute acid.…”

Section: Fragmentation Of Bp (Component 1)mentioning

confidence: 99%

“…The guinea pig peptide 79-88 differs from the corresponding bovine peptide by a single serine for proline substitution at position 79 (29). Peptide 64-73 was prepared by treating guinea pig peptide 43-88 with trypsin at an enzyme:substrate ratio of 1:50 at pH 8, 37°C for 4 h. The peptide was eluted from CM-cellulose at pH 4 with a NaC1 gradient and was further purified on Sephadex G25 (14). Peptide 64-73 has the same amino acid sequence in bovine and guinea pig BP (29).…”

Section: Fragmentation Of Bp (Component 1)mentioning

confidence: 99%

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Molecular internalization of a region of myelin basic protein

Whitaker¹,

Chou²,

Chou³

et al. 1977

The Journal of Experimental Medicine

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The conformation of myelin encephalitogenic or basic protein (BP) was investigated with a double-antibody radioimmunoassay by studying the reaction of BP or its fragments with antibodies produced in two rabbits against peptide 43-88 linked to rabbit serum albumin. Both antisera reacted well with peptide 43-88 but showed little or no reaction with BP. Absorption of these antisera with a BP-immunoadsorbent did not remove the antibody activity against peptide 43-88. Within the region of peptide 43- 88 it was shown that peptides 68-88 and 79-88 gave an equivalent or better reaction than peptide 43-88, whereas peptides 43-67 and 64-73 had very little reactivity. In the BP fragments containing region 43-88, peptide 1-88 showed the best reactivity, peptide 20-166 showed minimal reactivity, while peptide 1-115 showed none. These data document the internal position of at least a portion of peptide 43-88 and all of residues 79-88 in the BP molecule. The much greater reactivity of peptide 1-88 as compared to peptide 1-115 suggests that the region or a portion of the region of BP containing residues 89- 115 participates in the conformational alignment of BP restricting access to peptide 79-88. After absorption with BP, neither of the antisera prepared to peptide 43-88 reacted with PNS myelin in fixed tissue sections but continued to react with CNS myelin in similarly treated sections. The present findings demonstrate the need to consider the role of shielded antigenic determinants in the investigation of antigens or of immune responses.

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THE MAJOR SITE OF GUINEA‐PIG MYELIN BASIC PROTEIN ENCEPHALITOGENIC IN LEWIS RATS¹²

Cited by 109 publications

References 15 publications

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

Molecular internalization of a region of myelin basic protein

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THE MAJOR SITE OF GUINEA‐PIG MYELIN BASIC PROTEIN ENCEPHALITOGENIC IN LEWIS RATS12

Cited by 109 publications

References 15 publications

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

Molecular internalization of a region of myelin basic protein

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THE MAJOR SITE OF GUINEA‐PIG MYELIN BASIC PROTEIN ENCEPHALITOGENIC IN LEWIS RATS¹²