The global distribution and diversity of protein vaccine candidate antigens in the highly virulent Streptococcus pnuemoniae serotype:
- Cornick, Jennifer E, Tastan Bishop, Özlem, Yalcin, Feyruz, Kiran, Anmol M, Kumwenda, Benjamin, Chaguza, Chrispin, Govindpershad, Shanil, Ousmane, Sani, Senghore, Madikay, du Plessis, Mignon, Pluschke, Gerd, 1952-, Ebruke, Chinelo, McGee, Lesley, Sigaùque , Beutel, Collard, Jean-Marc, Bentley, Stephen D, Kadioglu , Aras, Antonio, Martin, von Gottberg, Anne, French, Neil, Klugman, Keith P, Heyderman, Robert S, Alderson, Mark, Everett, Dean B
- Authors: Cornick, Jennifer E , Tastan Bishop, Özlem , Yalcin, Feyruz , Kiran, Anmol M , Kumwenda, Benjamin , Chaguza, Chrispin , Govindpershad, Shanil , Ousmane, Sani , Senghore, Madikay , du Plessis, Mignon , Pluschke, Gerd, 1952- , Ebruke, Chinelo , McGee, Lesley , Sigaùque , Beutel , Collard, Jean-Marc , Bentley, Stephen D , Kadioglu , Aras , Antonio, Martin , von Gottberg, Anne , French, Neil , Klugman, Keith P , Heyderman, Robert S , Alderson, Mark , Everett, Dean B
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148318 , vital:38729 , DOI: 10.1016/j.vaccine.2016.12.037
- Description: Serotype 1 is one of the most common causes of pneumococcal disease worldwide. Pneumococcal protein vaccines are currently being developed as an alternate intervention strategy to pneumococcal conjugate vaccines. Pre-requisites for an efficacious pneumococcal protein vaccine are universal presence and minimal variation of the target antigen in the pneumococcal population, and the capability to induce a robust human immune response. We used in silico analysis to assess the prevalence of seven protein vaccine candidates (CbpA, PcpA, PhtD, PspA, SP0148, SP1912, SP2108) among 445 serotype 1 pneumococci from 26 different countries, across four continents. CbpA (76%), PspA (68%), PhtD (28%), PcpA (11%) were not universally encoded in the study population, and would not provide full coverage against serotype 1.
- Full Text:
- Date Issued: 2017
- Authors: Cornick, Jennifer E , Tastan Bishop, Özlem , Yalcin, Feyruz , Kiran, Anmol M , Kumwenda, Benjamin , Chaguza, Chrispin , Govindpershad, Shanil , Ousmane, Sani , Senghore, Madikay , du Plessis, Mignon , Pluschke, Gerd, 1952- , Ebruke, Chinelo , McGee, Lesley , Sigaùque , Beutel , Collard, Jean-Marc , Bentley, Stephen D , Kadioglu , Aras , Antonio, Martin , von Gottberg, Anne , French, Neil , Klugman, Keith P , Heyderman, Robert S , Alderson, Mark , Everett, Dean B
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148318 , vital:38729 , DOI: 10.1016/j.vaccine.2016.12.037
- Description: Serotype 1 is one of the most common causes of pneumococcal disease worldwide. Pneumococcal protein vaccines are currently being developed as an alternate intervention strategy to pneumococcal conjugate vaccines. Pre-requisites for an efficacious pneumococcal protein vaccine are universal presence and minimal variation of the target antigen in the pneumococcal population, and the capability to induce a robust human immune response. We used in silico analysis to assess the prevalence of seven protein vaccine candidates (CbpA, PcpA, PhtD, PspA, SP0148, SP1912, SP2108) among 445 serotype 1 pneumococci from 26 different countries, across four continents. CbpA (76%), PspA (68%), PhtD (28%), PcpA (11%) were not universally encoded in the study population, and would not provide full coverage against serotype 1.
- Full Text:
- Date Issued: 2017
Analysis of protein thermostability enhancing factors in industrially important thermus bacteria species
- Kumwenda, Benjamin, Litthauer, Derek, Tastan Bishop, Özlem, Reva, Oleg
- Authors: Kumwenda, Benjamin , Litthauer, Derek , Tastan Bishop, Özlem , Reva, Oleg
- Date: 2013
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/123085 , vital:35404 , https://doi.10.4137/EBO.S12539
- Description: Elucidation of evolutionary factors that enhance protein thermostability is a critical problem and was the focus of this work on Thermus species. Pairs of orthologous sequences of T. scotoductus SA-01 and T. thermophilus HB27, with the largest negative minimum folding energy (MFE) as predicted by the UNAFold algorithm, were statistically analyzed. Favored substitutions of amino acids residues and their properties were determined. Substitutions were analyzed in modeled protein structures to determine their locations and contribution to energy differences using PyMOL and FoldX programs respectively. Dominant trends in amino acid substitutions consistent with differences in thermostability between orthologous sequences were observed. T. thermophilus thermophilic proteins showed an increase in non-polar, tiny, and charged amino acids. An abundance of alanine substituted by serine and threonine, as well as arginine substituted by glutamine and lysine was observed in T. thermophilus HB27. Structural comparison showed that stabilizing mutations occurred on surfaces and loops in protein structures.
- Full Text:
- Date Issued: 2013
- Authors: Kumwenda, Benjamin , Litthauer, Derek , Tastan Bishop, Özlem , Reva, Oleg
- Date: 2013
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/123085 , vital:35404 , https://doi.10.4137/EBO.S12539
- Description: Elucidation of evolutionary factors that enhance protein thermostability is a critical problem and was the focus of this work on Thermus species. Pairs of orthologous sequences of T. scotoductus SA-01 and T. thermophilus HB27, with the largest negative minimum folding energy (MFE) as predicted by the UNAFold algorithm, were statistically analyzed. Favored substitutions of amino acids residues and their properties were determined. Substitutions were analyzed in modeled protein structures to determine their locations and contribution to energy differences using PyMOL and FoldX programs respectively. Dominant trends in amino acid substitutions consistent with differences in thermostability between orthologous sequences were observed. T. thermophilus thermophilic proteins showed an increase in non-polar, tiny, and charged amino acids. An abundance of alanine substituted by serine and threonine, as well as arginine substituted by glutamine and lysine was observed in T. thermophilus HB27. Structural comparison showed that stabilizing mutations occurred on surfaces and loops in protein structures.
- Full Text:
- Date Issued: 2013
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