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PMID |
Sentence |
1 |
8005685
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The results reported here show that the two meningococcal transferrin-binding proteins (TBP1 and TBP2) generate different immune responses in different host species and that there is variation in response dependent on the method of antigen preparation and possibly the route of administration.
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2 |
8535148
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Neisseria meningitidis strains grown under iron starvation conditions produce transferrin binding proteins (Tbp1 and Tbp2) which have been shown to play a major role in iron acquisition.
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3 |
8578805
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During iron-limited growth Neisseria meningitidis expresses two transferrin binding proteins, TBP1 and TBP2, with molecular masses of approximately 98 and 65-90 kDa depending on strain.
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4 |
8578805
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Mixtures of TBP1 and TBP2 (TBP1 + 2) from three meningococcal strains were purified using affinity chromatography and used to determine anti-TBP antibodies in human sera by ELISA.
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5 |
8578805
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Antibodies to separately purified TBP1 and TBP2 were also detected in both cases and carriers.
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6 |
8578805
|
During iron-limited growth Neisseria meningitidis expresses two transferrin binding proteins, TBP1 and TBP2, with molecular masses of approximately 98 and 65-90 kDa depending on strain.
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7 |
8578805
|
Mixtures of TBP1 and TBP2 (TBP1 + 2) from three meningococcal strains were purified using affinity chromatography and used to determine anti-TBP antibodies in human sera by ELISA.
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8 |
8578805
|
Antibodies to separately purified TBP1 and TBP2 were also detected in both cases and carriers.
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9 |
8578805
|
During iron-limited growth Neisseria meningitidis expresses two transferrin binding proteins, TBP1 and TBP2, with molecular masses of approximately 98 and 65-90 kDa depending on strain.
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10 |
8578805
|
Mixtures of TBP1 and TBP2 (TBP1 + 2) from three meningococcal strains were purified using affinity chromatography and used to determine anti-TBP antibodies in human sera by ELISA.
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11 |
8578805
|
Antibodies to separately purified TBP1 and TBP2 were also detected in both cases and carriers.
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12 |
8606350
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Iron-regulated outer-membrane proteins have attracted considerable attention in recent years and it has become increasingly evident that the meningococcal transferrin-binding proteins, TBP1 and TBP2, have characteristics compatible with a safe and broadly cross-reactive vaccine candidate.
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13 |
8606350
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In this review, the structure-function and immunological properties of TBP1 and TBP2 are discussed.
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14 |
8606350
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Iron-regulated outer-membrane proteins have attracted considerable attention in recent years and it has become increasingly evident that the meningococcal transferrin-binding proteins, TBP1 and TBP2, have characteristics compatible with a safe and broadly cross-reactive vaccine candidate.
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15 |
8606350
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In this review, the structure-function and immunological properties of TBP1 and TBP2 are discussed.
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16 |
8821649
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When grown in vivo, or under iron-restriction in vitro, Neisseria meningitidis expresses a number of iron-regulated outer membrane proteins, including two transferrin-binding proteins (Tbp1 and Tbp2).
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17 |
8821649
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We have previously raised rabbit and murine polyclonal monospecific antisera against the Tbps of strain SD (B:15:P1.16) which showed varying degrees of cross-reactivity on immunoblots between the Tbp1 and/or Tbp2 molecules of different heterologous strains from various serogroups, types and subtypes.
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18 |
8821649
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Furthermore, the rabbit antiserum was able to kill both Tbp1 and Tbp2 mutants of strain B16B6 (B2a:P1.2) to almost the same level as the wild type strain, indicating that both components of the transferrin receptor (Tbp1 and Tbp2) are most likely to be surface accessible and capable of generating bactericidal antibodies which can kill homologous and heterologous strains.
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19 |
8821649
|
When grown in vivo, or under iron-restriction in vitro, Neisseria meningitidis expresses a number of iron-regulated outer membrane proteins, including two transferrin-binding proteins (Tbp1 and Tbp2).
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20 |
8821649
|
We have previously raised rabbit and murine polyclonal monospecific antisera against the Tbps of strain SD (B:15:P1.16) which showed varying degrees of cross-reactivity on immunoblots between the Tbp1 and/or Tbp2 molecules of different heterologous strains from various serogroups, types and subtypes.
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21 |
8821649
|
Furthermore, the rabbit antiserum was able to kill both Tbp1 and Tbp2 mutants of strain B16B6 (B2a:P1.2) to almost the same level as the wild type strain, indicating that both components of the transferrin receptor (Tbp1 and Tbp2) are most likely to be surface accessible and capable of generating bactericidal antibodies which can kill homologous and heterologous strains.
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22 |
8821649
|
When grown in vivo, or under iron-restriction in vitro, Neisseria meningitidis expresses a number of iron-regulated outer membrane proteins, including two transferrin-binding proteins (Tbp1 and Tbp2).
|
23 |
8821649
|
We have previously raised rabbit and murine polyclonal monospecific antisera against the Tbps of strain SD (B:15:P1.16) which showed varying degrees of cross-reactivity on immunoblots between the Tbp1 and/or Tbp2 molecules of different heterologous strains from various serogroups, types and subtypes.
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24 |
8821649
|
Furthermore, the rabbit antiserum was able to kill both Tbp1 and Tbp2 mutants of strain B16B6 (B2a:P1.2) to almost the same level as the wild type strain, indicating that both components of the transferrin receptor (Tbp1 and Tbp2) are most likely to be surface accessible and capable of generating bactericidal antibodies which can kill homologous and heterologous strains.
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25 |
8965674
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Some of these proteins e.g. transferrin-binding proteins 1 and 2 (Tbp1 and Tbp2), are required for the acquisition of iron from transferrin and are examples of important iron-regulated meningococcal surface antigens which are not expressed after growth in common laboratory media.
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26 |
8965674
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Inhibition of iron uptake from citrate was unaffected which suggests that this effect is due to antibodies against the components of the transferrin binding system, specially Tbp2.
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27 |
9004513
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This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
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28 |
9004513
|
Whole cells of all type b and non-typable strains examined bound human transferrin; whilst most strains possessed a Tbp1 of approximately 105 kDa, the molecular mass of Tbp2 varied from 79 to 94 kDa.
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29 |
9004513
|
Antisera raised against affinity-purified native H. influenzae Tbp1/Tbp2 receptor complex cross-reacted on Western blots with the respective Tbps of all the Haemophilus strains examined.
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30 |
9004513
|
When used to probe Neisseria meningitidis Tbps, sera from each of four mice immunized with the Haemophilus Tbp1/2 complex recognized the 68 kDa Tbp2 of N. meningitidis strain B16B6 but not the 78 kDa Tbp2 of N. meningitidis strain 70942.
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31 |
9004513
|
Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
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32 |
9004513
|
This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
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33 |
9004513
|
Whole cells of all type b and non-typable strains examined bound human transferrin; whilst most strains possessed a Tbp1 of approximately 105 kDa, the molecular mass of Tbp2 varied from 79 to 94 kDa.
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34 |
9004513
|
Antisera raised against affinity-purified native H. influenzae Tbp1/Tbp2 receptor complex cross-reacted on Western blots with the respective Tbps of all the Haemophilus strains examined.
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35 |
9004513
|
When used to probe Neisseria meningitidis Tbps, sera from each of four mice immunized with the Haemophilus Tbp1/2 complex recognized the 68 kDa Tbp2 of N. meningitidis strain B16B6 but not the 78 kDa Tbp2 of N. meningitidis strain 70942.
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36 |
9004513
|
Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
|
37 |
9004513
|
This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
|
38 |
9004513
|
Whole cells of all type b and non-typable strains examined bound human transferrin; whilst most strains possessed a Tbp1 of approximately 105 kDa, the molecular mass of Tbp2 varied from 79 to 94 kDa.
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39 |
9004513
|
Antisera raised against affinity-purified native H. influenzae Tbp1/Tbp2 receptor complex cross-reacted on Western blots with the respective Tbps of all the Haemophilus strains examined.
|
40 |
9004513
|
When used to probe Neisseria meningitidis Tbps, sera from each of four mice immunized with the Haemophilus Tbp1/2 complex recognized the 68 kDa Tbp2 of N. meningitidis strain B16B6 but not the 78 kDa Tbp2 of N. meningitidis strain 70942.
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41 |
9004513
|
Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
|
42 |
9004513
|
This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
|
43 |
9004513
|
Whole cells of all type b and non-typable strains examined bound human transferrin; whilst most strains possessed a Tbp1 of approximately 105 kDa, the molecular mass of Tbp2 varied from 79 to 94 kDa.
|
44 |
9004513
|
Antisera raised against affinity-purified native H. influenzae Tbp1/Tbp2 receptor complex cross-reacted on Western blots with the respective Tbps of all the Haemophilus strains examined.
|
45 |
9004513
|
When used to probe Neisseria meningitidis Tbps, sera from each of four mice immunized with the Haemophilus Tbp1/2 complex recognized the 68 kDa Tbp2 of N. meningitidis strain B16B6 but not the 78 kDa Tbp2 of N. meningitidis strain 70942.
|
46 |
9004513
|
Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
|
47 |
9004513
|
This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
|
48 |
9004513
|
Whole cells of all type b and non-typable strains examined bound human transferrin; whilst most strains possessed a Tbp1 of approximately 105 kDa, the molecular mass of Tbp2 varied from 79 to 94 kDa.
|
49 |
9004513
|
Antisera raised against affinity-purified native H. influenzae Tbp1/Tbp2 receptor complex cross-reacted on Western blots with the respective Tbps of all the Haemophilus strains examined.
|
50 |
9004513
|
When used to probe Neisseria meningitidis Tbps, sera from each of four mice immunized with the Haemophilus Tbp1/2 complex recognized the 68 kDa Tbp2 of N. meningitidis strain B16B6 but not the 78 kDa Tbp2 of N. meningitidis strain 70942.
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51 |
9004513
|
Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
|