A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C
The protein composition of an Outer Membrane Vesicle (OMV) preparation that constitutes the active pharmaceutical ingredient of VA-MENGOC-BC®, an effective vaccine against Neisseria meningitidis serogroups B, and C is presented. This preparation has a high lipid content and five abundant membrane pr...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2017-11-01
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| Series: | Human Vaccines & Immunotherapeutics |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/21645515.2017.1356961 |
| _version_ | 1797677567178702848 |
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| author | Yordanka Masforrol Jeovanis Gil Darien García Jesús Noda Yassel Ramos Lázaro Betancourt Osmany Guirola Sonia González Boris Acevedo Vladimir Besada Osvaldo Reyes Luis Javier González |
| author_facet | Yordanka Masforrol Jeovanis Gil Darien García Jesús Noda Yassel Ramos Lázaro Betancourt Osmany Guirola Sonia González Boris Acevedo Vladimir Besada Osvaldo Reyes Luis Javier González |
| author_sort | Yordanka Masforrol |
| collection | DOAJ |
| description | The protein composition of an Outer Membrane Vesicle (OMV) preparation that constitutes the active pharmaceutical ingredient of VA-MENGOC-BC®, an effective vaccine against Neisseria meningitidis serogroups B, and C is presented. This preparation has a high lipid content and five abundant membrane proteins (FetA, PorA, PorB, RmpM, and Opc), constituting approximately 70% of the total protein mass. The protein composition was determined by combining the use of the Hexapeptide Ligand Library and an orthogonal tandem fractionation of tryptic peptides by reverse-phase chromatography at alkaline and acid pH. This approach equalizes the concentration of tryptic peptides derived from low- and high-abundance proteins as well as considerably simplifying the number of peptides analyzed by LC-MS/MS, enhancing the possibility of identifying low-abundance species. Fifty-one percent of the proteins originally annotated as membrane proteins in the genome of the MC58 strain were identified. One hundred and sixty-eight low-abundance cytosolic proteins presumably occluded within OMV were also identified. Four (NadA, NUbp, GNA2091, and fHbp), out of the five antigens constituting the Bexsero® vaccine, were detected in this OMV preparation. In particular, fHbp is also the active principle of the Trumenba® vaccine developed by Pfizer. The HpuA and HpuB gene products (not annotated in the MC58 genome) were identified in the CU385 strain, a clinical isolate that is used to produce this OMV. Considering the proteins identified here and previous work done by our group, the protein catalogue of this OMV preparation was extended to 266 different protein species. |
| first_indexed | 2024-03-11T22:47:10Z |
| format | Article |
| id | doaj.art-b02c5e4d51334d42b203330fb7b5e7d5 |
| institution | Directory Open Access Journal |
| issn | 2164-5515 2164-554X |
| language | English |
| last_indexed | 2024-03-11T22:47:10Z |
| publishDate | 2017-11-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Human Vaccines & Immunotherapeutics |
| spelling | doaj.art-b02c5e4d51334d42b203330fb7b5e7d52023-09-22T08:17:51ZengTaylor & Francis GroupHuman Vaccines & Immunotherapeutics2164-55152164-554X2017-11-0113112548256010.1080/21645515.2017.13569611356961A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and CYordanka Masforrol0Jeovanis Gil1Darien García2Jesús Noda3Yassel Ramos4Lázaro Betancourt5Osmany Guirola6Sonia González7Boris Acevedo8Vladimir Besada9Osvaldo Reyes10Luis Javier González11Peptide Synthesis Group, Center for Genetic Engineering and BiotechnologyCenter for Genetic Engineering and BiotechnologyVaccine Department, Center for Genetic Engineering and BiotechnologyCenter for Genetic Engineering and BiotechnologyCenter for Genetic Engineering and BiotechnologyCenter for Genetic Engineering and BiotechnologyBioinformatics Department, Center for Genetic Engineering and BiotechnologyVaccine Department, Center for Genetic Engineering and BiotechnologyQuality Assurance Departments, Center for Genetic Engineering and Biotechnology,Center for Genetic Engineering and BiotechnologyPeptide Synthesis Group, Center for Genetic Engineering and BiotechnologyCenter for Genetic Engineering and BiotechnologyThe protein composition of an Outer Membrane Vesicle (OMV) preparation that constitutes the active pharmaceutical ingredient of VA-MENGOC-BC®, an effective vaccine against Neisseria meningitidis serogroups B, and C is presented. This preparation has a high lipid content and five abundant membrane proteins (FetA, PorA, PorB, RmpM, and Opc), constituting approximately 70% of the total protein mass. The protein composition was determined by combining the use of the Hexapeptide Ligand Library and an orthogonal tandem fractionation of tryptic peptides by reverse-phase chromatography at alkaline and acid pH. This approach equalizes the concentration of tryptic peptides derived from low- and high-abundance proteins as well as considerably simplifying the number of peptides analyzed by LC-MS/MS, enhancing the possibility of identifying low-abundance species. Fifty-one percent of the proteins originally annotated as membrane proteins in the genome of the MC58 strain were identified. One hundred and sixty-eight low-abundance cytosolic proteins presumably occluded within OMV were also identified. Four (NadA, NUbp, GNA2091, and fHbp), out of the five antigens constituting the Bexsero® vaccine, were detected in this OMV preparation. In particular, fHbp is also the active principle of the Trumenba® vaccine developed by Pfizer. The HpuA and HpuB gene products (not annotated in the MC58 genome) were identified in the CU385 strain, a clinical isolate that is used to produce this OMV. Considering the proteins identified here and previous work done by our group, the protein catalogue of this OMV preparation was extended to 266 different protein species.http://dx.doi.org/10.1080/21645515.2017.1356961omvvaccineneisseria meningitidispeptide libraryequalizationproteomicsdynamic concentration rangevamengo bc |
| spellingShingle | Yordanka Masforrol Jeovanis Gil Darien García Jesús Noda Yassel Ramos Lázaro Betancourt Osmany Guirola Sonia González Boris Acevedo Vladimir Besada Osvaldo Reyes Luis Javier González A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C Human Vaccines & Immunotherapeutics omv vaccine neisseria meningitidis peptide library equalization proteomics dynamic concentration range vamengo bc |
| title | A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C |
| title_full | A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C |
| title_fullStr | A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C |
| title_full_unstemmed | A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C |
| title_short | A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C |
| title_sort | deeper mining on the protein composition of va mengoc bc r an omv based vaccine against n meningitidis serogroup b and c |
| topic | omv vaccine neisseria meningitidis peptide library equalization proteomics dynamic concentration range vamengo bc |
| url | http://dx.doi.org/10.1080/21645515.2017.1356961 |
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