Structural analysis of an outer surface protein from the Lyme disease spirochete, Borrelia burgdorferi, using circular dichroism and fluorescence spectroscopy

France, L.; Kieleczawa, Jan; Dunn, John J.; Hínd, Geoffrey; Sutherland, John C.

doi:10.1016/0167-4838(92)90424-c

Cited by 23 publications

(10 citation statements)

References 29 publications

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“…Optical path lengths were varied from 4 ,um to 1 mm; a Gray cell (10) was used to obtain path lengths < 100 ,um. The spectrometer and optical path lengths were calibrated as described (11 (Fig. 1A), structural analysis of the CD spectra shows no significant differences among the peptides, which consist predominantly of 8A-strands (--28%), (3-turns (=23%), and "other" structures (-39%), as expected for random-coil peptides (17).…”

Section: Methodsmentioning

confidence: 84%

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

France

Piatti

Newman

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Section: Methodsmentioning

confidence: 84%

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

France

Piatti

Newman

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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“…A large electrostatic component to the folding of recombinant OspA had been predicted based on the unusual stability of the protein at low and high salt concentrations and over a wide pH range (32). In our model, all but three of 74 charged residues have surface-exposed charged groups forming ion pairs or higher-order arrays (the three exceptions are discussed later).…”

Section: H ͉Fp(h) ϫ Fph(h)͉͞•h Fp(h)mentioning

confidence: 93%

Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab

Dunn

Luft

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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153

163

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OspA (outer surface protein A) is an abundant immunogenic lipoprotein of the Lyme disease spirochete Borrelia burgdorferi. The crystal structure of a soluble recombinant form of OspA was solved in a complex with the Fab fragment of mouse monoclonal antibody 184.1 and refined to a resolution of 1.9 Å. OspA has a repetitive antiparallel ␤ topology with an unusual nonglobular region of ''freestanding'' sheet connecting globular N-and C-terminal domains. Arrays of residues with alternating charges are a predominant feature of the folding pattern in the nonglobular region. The 184.1 epitope overlaps with a well conserved surface in the N-terminal domain, and a hydrophobic cavity buried in a positively charged cleft in the C-terminal domain is a potential binding site for an unknown ligand. An exposed variable region on the C-terminal domain of OspA is predicted to be an important factor in the worldwide effectiveness of OspA-based vaccines.

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“…5C ). Additionally, the Far-UV CD spectra of rStI, StI W111C monomer and dimer, recorded in the range 20–90 °C, do not present an isodichroic point 55 , 56 (Fig. 5A–C ).…”

Section: Resultsmentioning

confidence: 94%

Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation

Valle

Socas

Canet

et al. 2018

Sci Rep

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The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate that monomers and dimers are the only independent oligomeric states encountered. Indeed, circular dichroism and fluorescence spectroscopies showed that Trp/Tyr residues participate in homodimerization and that the dimer is less thermostable than the monomer. A homodimer three-dimensional model was constructed and indicates that Trp147/Tyr137 are at the homodimer interface. Spectroscopy results validated the 3D-model and assigned 85° to the disulfide bridge dihedral angle responsible for dimerization. The homodimer model suggests that alterations in the membrane/carbohydrate-binding sites in one of the monomers, as result of dimerization, could explain the decrease in the homodimer ability to form pores.

show abstract

Structural analysis of an outer surface protein from the Lyme disease spirochete, Borrelia burgdorferi, using circular dichroism and fluorescence spectroscopy

Cited by 23 publications

References 29 publications

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab

Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation

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