Ignet

Gene Information

Gene symbol: TBPL2

Gene name: TATA box binding protein like 2

HGNC ID: 19841

Synonyms: TRF3, TBP2

Related Genes

#	Gene Symbol	Number of hits
1	LTF	1 hits
2	PSMC3	1 hits
3	TF	1 hits
4	TFRC	1 hits

Related Sentences

#	PMID	Sentence
1	1612755	The antigenicity of N. meningitidis 37- and 70-kDa IROMPs has been studied previously; in this work, we studied the immunogenicity and antigenic heterogeneity of another IROMP, the human transferrin-binding protein 2 (TBP2), which seems to be indispensable for meningococcal growth inside the host.
2	7752881	Whereas the LbpA protein shows homology to the transferrin-binding protein 1 (Tbp1), the putative protein encoded by the open reading frame upstream of IbpA shows extensive homology to Tbp2, suggesting that iron-acquisition from lactoferrin, like from transferrin, requires two specific proteins in the outer membrane.
3	7866351	However, the response to one of the major iron-regulated outer membrane antigens, the transferrin binding protein 2 (TBP2), was unaffected by the culture medium or the model, human or mouse, used for the analysis.
4	8005685	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.
5	8156052	Our results demonstrate that transferrin-binding protein 2 (TBP2) is immunogenic in humans, to varying degrees depending on the strain, and that TBP2s (like the equivalent proteins of Haemophilus influenzae type b) are among the most important iron-regulated outer membrane antigens expressed during infection.
6	8535148	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.
7	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.
8	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.
9	8578805	Antibodies to separately purified TBP1 and TBP2 were also detected in both cases and carriers.
10	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.
11	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.
12	8578805	Antibodies to separately purified TBP1 and TBP2 were also detected in both cases and carriers.
13	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.
14	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.
15	8578805	Antibodies to separately purified TBP1 and TBP2 were also detected in both cases and carriers.
16	8606350	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.
17	8606350	In this review, the structure-function and immunological properties of TBP1 and TBP2 are discussed.
18	8606350	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.
19	8606350	In this review, the structure-function and immunological properties of TBP1 and TBP2 are discussed.
20	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).
21	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.
22	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.
23	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).
24	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.
25	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.
26	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).
27	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.
28	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.
29	8965674	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.
30	8965674	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.
31	8965674	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.
32	8965674	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.
33	9004513	This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
34	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.
35	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.
36	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.
37	9004513	Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
38	9004513	This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
39	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.
40	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.
41	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.
42	9004513	Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
43	9004513	This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
44	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.
45	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.
46	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.
47	9004513	Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
48	9004513	This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
49	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.
50	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.
51	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.
52	9004513	Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.
53	9004513	This involves two outer-membrane transferrin-binding proteins (Tbps) termed Tbp1 and Tbp2 which show considerable preference for the human form of transferrin.
54	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.
55	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.
56	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.
57	9004513	Sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis.