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Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4
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| Zeitschriftentitel: | Biochemical Journal |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Biochemical Journal, 232, 1985, 2, S. 513-519 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
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| Schlagwörter: |
| author_facet |
Aubert, B Chesne, S Arlaud, G J Colomb, M G Aubert, B Chesne, S Arlaud, G J Colomb, M G |
|---|---|
| author |
Aubert, B Chesne, S Arlaud, G J Colomb, M G |
| spellingShingle |
Aubert, B Chesne, S Arlaud, G J Colomb, M G Biochemical Journal Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 Cell Biology Molecular Biology Biochemistry |
| author_sort |
aubert, b |
| spelling |
Aubert, B Chesne, S Arlaud, G J Colomb, M G 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2320513 <jats:p>The heptoseless mutant of Escherichia coli, E. coli D31 m4, binds C1q and C1 at 0 degrees C and at low ionic strength (I0.07). Under these conditions, the maximum C1q binding averages 3.0 × 10(5) molecules per bacterium, with a Ka of 1.4 × 10(8) M-1. Binding involves the collagen-like region of C1q, as shown by the capacity of C1q pepsin-digest fragments to bind to E. coli D31 m4, and to compete with native C1q. Proenzyme and activated forms of C1 subcomponents C1r and C1s and their Ca2+-dependent association (C1r-C1s)2 do not bind to E. coli D31 m4. In contrast, the C1 complex binds very effectively, with an average fixation of 3.5 × 10(5) molecules per bacterium, and a Ka of 0.25 × 10(8) M-1, both comparable with the values obtained for C1q binding. C1 bound to E. coli D31 m4 undergoes rapid activation at 0 degrees C. The activation process is not affected by C1-inhibitor, and only slightly inhibited by p-nitrophenyl p'-guanidinobenzoate. No turnover of the (C1r-C1s)2 subunit is observed. Once activated, C1 is only partially dissociated by C1-inhibitor. Our observations are in favour of a strong association between C1 and the outer membrane of E. coli D31 m4, involving mainly the collagen-like moiety of C1.</jats:p> Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of <i>Escherichia coli</i> D31 m4 Biochemical Journal |
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Portland Press Ltd., 1985 |
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Portland Press Ltd., 1985 |
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0264-6021 1470-8728 |
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1985 |
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Biochemical Journal |
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49 |
| title |
Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_unstemmed |
Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_full |
Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_fullStr |
Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_full_unstemmed |
Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_short |
Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_sort |
antibody-independent interaction between the first component of human complement, c1, and the outer membrane of <i>escherichia coli</i> d31 m4 |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1042/bj2320513 |
| publishDate |
1985 |
| physical |
513-519 |
| description |
<jats:p>The heptoseless mutant of Escherichia coli, E. coli D31 m4, binds C1q and C1 at 0 degrees C and at low ionic strength (I0.07). Under these conditions, the maximum C1q binding averages 3.0 × 10(5) molecules per bacterium, with a Ka of 1.4 × 10(8) M-1. Binding involves the collagen-like region of C1q, as shown by the capacity of C1q pepsin-digest fragments to bind to E. coli D31 m4, and to compete with native C1q. Proenzyme and activated forms of C1 subcomponents C1r and C1s and their Ca2+-dependent association (C1r-C1s)2 do not bind to E. coli D31 m4. In contrast, the C1 complex binds very effectively, with an average fixation of 3.5 × 10(5) molecules per bacterium, and a Ka of 0.25 × 10(8) M-1, both comparable with the values obtained for C1q binding. C1 bound to E. coli D31 m4 undergoes rapid activation at 0 degrees C. The activation process is not affected by C1-inhibitor, and only slightly inhibited by p-nitrophenyl p'-guanidinobenzoate. No turnover of the (C1r-C1s)2 subunit is observed. Once activated, C1 is only partially dissociated by C1-inhibitor. Our observations are in favour of a strong association between C1 and the outer membrane of E. coli D31 m4, involving mainly the collagen-like moiety of C1.</jats:p> |
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| author | Aubert, B, Chesne, S, Arlaud, G J, Colomb, M G |
| author_facet | Aubert, B, Chesne, S, Arlaud, G J, Colomb, M G, Aubert, B, Chesne, S, Arlaud, G J, Colomb, M G |
| author_sort | aubert, b |
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| description | <jats:p>The heptoseless mutant of Escherichia coli, E. coli D31 m4, binds C1q and C1 at 0 degrees C and at low ionic strength (I0.07). Under these conditions, the maximum C1q binding averages 3.0 × 10(5) molecules per bacterium, with a Ka of 1.4 × 10(8) M-1. Binding involves the collagen-like region of C1q, as shown by the capacity of C1q pepsin-digest fragments to bind to E. coli D31 m4, and to compete with native C1q. Proenzyme and activated forms of C1 subcomponents C1r and C1s and their Ca2+-dependent association (C1r-C1s)2 do not bind to E. coli D31 m4. In contrast, the C1 complex binds very effectively, with an average fixation of 3.5 × 10(5) molecules per bacterium, and a Ka of 0.25 × 10(8) M-1, both comparable with the values obtained for C1q binding. C1 bound to E. coli D31 m4 undergoes rapid activation at 0 degrees C. The activation process is not affected by C1-inhibitor, and only slightly inhibited by p-nitrophenyl p'-guanidinobenzoate. No turnover of the (C1r-C1s)2 subunit is observed. Once activated, C1 is only partially dissociated by C1-inhibitor. Our observations are in favour of a strong association between C1 and the outer membrane of E. coli D31 m4, involving mainly the collagen-like moiety of C1.</jats:p> |
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| imprint | Portland Press Ltd., 1985 |
| imprint_str_mv | Portland Press Ltd., 1985 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
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| physical | 513-519 |
| publishDate | 1985 |
| publishDateSort | 1985 |
| publisher | Portland Press Ltd. |
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| recordtype | ai |
| series | Biochemical Journal |
| source_id | 49 |
| spelling | Aubert, B Chesne, S Arlaud, G J Colomb, M G 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2320513 <jats:p>The heptoseless mutant of Escherichia coli, E. coli D31 m4, binds C1q and C1 at 0 degrees C and at low ionic strength (I0.07). Under these conditions, the maximum C1q binding averages 3.0 × 10(5) molecules per bacterium, with a Ka of 1.4 × 10(8) M-1. Binding involves the collagen-like region of C1q, as shown by the capacity of C1q pepsin-digest fragments to bind to E. coli D31 m4, and to compete with native C1q. Proenzyme and activated forms of C1 subcomponents C1r and C1s and their Ca2+-dependent association (C1r-C1s)2 do not bind to E. coli D31 m4. In contrast, the C1 complex binds very effectively, with an average fixation of 3.5 × 10(5) molecules per bacterium, and a Ka of 0.25 × 10(8) M-1, both comparable with the values obtained for C1q binding. C1 bound to E. coli D31 m4 undergoes rapid activation at 0 degrees C. The activation process is not affected by C1-inhibitor, and only slightly inhibited by p-nitrophenyl p'-guanidinobenzoate. No turnover of the (C1r-C1s)2 subunit is observed. Once activated, C1 is only partially dissociated by C1-inhibitor. Our observations are in favour of a strong association between C1 and the outer membrane of E. coli D31 m4, involving mainly the collagen-like moiety of C1.</jats:p> Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of <i>Escherichia coli</i> D31 m4 Biochemical Journal |
| spellingShingle | Aubert, B, Chesne, S, Arlaud, G J, Colomb, M G, Biochemical Journal, Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4, Cell Biology, Molecular Biology, Biochemistry |
| title | Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_full | Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_fullStr | Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_full_unstemmed | Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_short | Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| title_sort | antibody-independent interaction between the first component of human complement, c1, and the outer membrane of <i>escherichia coli</i> d31 m4 |
| title_unstemmed | Antibody-independent interaction between the first component of human complement, C1, and the outer membrane of Escherichia coli D31 m4 |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1042/bj2320513 |