Gene for an immunoglobulin-binding protein from a group G streptococcus

Fahnestock, Stephen R.; Alexander, Patrick; Nagle, James W.; Filpula, David

doi:10.1128/jb.167.3.870-880.1986

Cited by 241 publications

(132 citation statements)

References 32 publications

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“…We chose the B1 domain of streptococcal protein G (GB1) (27) as our test protein because its structure, stability and folding kinetics have been extensively studied in dilute solution (28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38).…”

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confidence: 99%

Residue level quantification of protein stability in living cells

Monteith¹,

Pielak

2014

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

107

178

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Significance Proteins function in a sea of macromolecules within cells, but are traditionally studied under ideal conditions in vitro . The more details we amass from experiments performed in cells, the closer we will get to understanding fundamental aspects of protein chemistry in the cellular environment. In addition to furthering our essential knowledge of biochemistry, advancements in the field of macromolecular crowding will drive efforts to stabilize protein-based therapeutics. Here, we show that protein stability can be measured at the residue level in living cells without adding destabilizing cosolutes or heat.

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mentioning

confidence: 99%

Residue level quantification of protein stability in living cells

Monteith¹,

Pielak

2014

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

107

178

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“…5), and estimations of M, in these systems are routinely based on the use of globular protein standards. Certainly, aberrant behaviour of other cell-wall-associated proteins during SDS-PAGE has been observed by several authors (Hartford et al, 1997;Jonsson et al, 1991;Hollingshead et al, 1986;Fahnestock et al, 1986) equi FgBP can this phenomenon be attributed to the presence of the putative wall-spanning domain, since in both cases the ratio of apparent to predicted M, is largely unaffected for recombinant truncates in which this region has been deleted or reduced in size ( Fig. 6 ; Hartford et al., 1997).…”

Section: Discussionmentioning

confidence: 99%

Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with Streptococcus equi subsp. equi

1998

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Cell-wall-associated proteins from Streptococcus equi subsp. equi, the causative agent of strangles, were analysed with a view to identifying a potential protective antigen. Preparations of these proteins, isolated from mutanolysin extracts of cell walls, were shown to contain one major high-M r protein species (apparent M r 220000 and 550000 when analysed by SDS-PAGE and gel-filtration chromatography, respectively). The high-M r protein bound horse fibrinogen and was purified under non-denaturing conditions using fibrinogen affinity chromatography. The fibrinogen-binding protein (FgBP) reacted with serum taken from horses recovering from strangles and protected mice against lethal challenge from S. equi subsp. equi. The sequence of the corresponding gene (fbp) was determined and shown to encode a mature protein (M r 54597) with predicted coiled-coil structure. An FgBP truncate, lacking the C-terminal cell wall/membrane anchor domain, was overexpressed in and purified from Escherichia coli and was shown to behave in an analogous fashion to the wild-type product in terms of M r estimation, fibrinogen binding and seroreactivity.

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“…Depending on the Streptococcus strain, SPG contains two or three immunoglobulin-binding domains of approximate 55 residues, denoted B1 through B3 or C1 through C3 by different authors [11][12][13] (Fig. la).…”

Section: Introductionmentioning

confidence: 99%