Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat
Pasteurella multocida (P. multocida) serotype B is associated with hemorrhagic septicaemia (HS) disease endemic in Africa, India and Asian countries. It is causative agent of thriftily significant disease in livestock. Hence, this study purposed and aimed to identify and express an immunogenic solub...
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| Format: | Thesis |
| Language: | English |
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2015
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| Online Access: | https://ir.uitm.edu.my/id/eprint/34756/1/34756.pdf |
| _version_ | 1825737994547494912 |
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| author | Jumahat, Noor Masyitah |
| author_facet | Jumahat, Noor Masyitah |
| author_sort | Jumahat, Noor Masyitah |
| collection | UITM |
| description | Pasteurella multocida (P. multocida) serotype B is associated with hemorrhagic septicaemia (HS) disease endemic in Africa, India and Asian countries. It is causative agent of thriftily significant disease in livestock. Hence, this study purposed and aimed to identify and express an immunogenic soluble protein of P. multocida in efforts toward development of HS vaccine. Immunogenic - soluble protein was identified as lipoprotein B (plpB) using electrospray mass spectrometry. The size of expressed purified recombinant protein was approximately 39kDa. Immunogenicity study of the recombinant protein plpB was carried out using 6 groups of BALB/c mice. The groups were immunized with recombinant protein (Group 1), soluble recombinant protein (Group 2), insoluble recombinant protein (Group 3), vector (Group 4), soluble protein of P. multocida (Group 5) and PBS (Group 6) respectively. Mice in group 4 and 6 showed signs and symptom of HS after challenge with the parental strain (p-value < 0.05). However, immunised mice with purified recombinant protein did not show signs and symptoms of HS. Based on immunoblotting analysis, purified recombinant protein was significantly immunogenic (p-value < 0.05). Additionally, no inflammation was seen in the tissues of organs from mice immunized with purified recombinant protein, which indicates that recombinant protein was 100% protective towards P. multocida infection and eventually towards HS disease. Thus, this study shows that the recombinant protein lipoprotein B (plpB) is significantly immunogenic and could be a potential candidate in developing vaccine against HS. |
| first_indexed | 2024-03-06T02:26:51Z |
| format | Thesis |
| id | oai:ir.uitm.edu.my:34756 |
| institution | Universiti Teknologi MARA |
| language | English |
| last_indexed | 2024-03-06T02:26:51Z |
| publishDate | 2015 |
| record_format | dspace |
| spelling | oai:ir.uitm.edu.my:347562021-11-09T02:58:54Z https://ir.uitm.edu.my/id/eprint/34756/ Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat Jumahat, Noor Masyitah Immunology Immunochemistry Pasteurella multocida (P. multocida) serotype B is associated with hemorrhagic septicaemia (HS) disease endemic in Africa, India and Asian countries. It is causative agent of thriftily significant disease in livestock. Hence, this study purposed and aimed to identify and express an immunogenic soluble protein of P. multocida in efforts toward development of HS vaccine. Immunogenic - soluble protein was identified as lipoprotein B (plpB) using electrospray mass spectrometry. The size of expressed purified recombinant protein was approximately 39kDa. Immunogenicity study of the recombinant protein plpB was carried out using 6 groups of BALB/c mice. The groups were immunized with recombinant protein (Group 1), soluble recombinant protein (Group 2), insoluble recombinant protein (Group 3), vector (Group 4), soluble protein of P. multocida (Group 5) and PBS (Group 6) respectively. Mice in group 4 and 6 showed signs and symptom of HS after challenge with the parental strain (p-value < 0.05). However, immunised mice with purified recombinant protein did not show signs and symptoms of HS. Based on immunoblotting analysis, purified recombinant protein was significantly immunogenic (p-value < 0.05). Additionally, no inflammation was seen in the tissues of organs from mice immunized with purified recombinant protein, which indicates that recombinant protein was 100% protective towards P. multocida infection and eventually towards HS disease. Thus, this study shows that the recombinant protein lipoprotein B (plpB) is significantly immunogenic and could be a potential candidate in developing vaccine against HS. 2015 Thesis NonPeerReviewed text en https://ir.uitm.edu.my/id/eprint/34756/1/34756.pdf Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat. (2015) Masters thesis, thesis, Universiti Teknologi MARA. |
| spellingShingle | Immunology Immunochemistry Jumahat, Noor Masyitah Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat |
| title | Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat |
| title_full | Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat |
| title_fullStr | Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat |
| title_full_unstemmed | Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat |
| title_short | Identification and immunogenicity study of soluble protein derived from Pasteurella multocida serotype B / Noor Masyitah Jumahat |
| title_sort | identification and immunogenicity study of soluble protein derived from pasteurella multocida serotype b noor masyitah jumahat |
| topic | Immunology Immunochemistry |
| url | https://ir.uitm.edu.my/id/eprint/34756/1/34756.pdf |
| work_keys_str_mv | AT jumahatnoormasyitah identificationandimmunogenicitystudyofsolubleproteinderivedfrompasteurellamultocidaserotypebnoormasyitahjumahat |