In silico design of an immunogen against Acinetobacter baumannii based on a novel model for native structure of Outer membrane protein A

Jahangiri, Abolfazl; Rasooli, Iraj; Owlia, Parviz; Fooladi, Abbas Ali Imani; Salimian, Jafar

doi:10.1016/j.micpath.2017.02.028

Cited by 51 publications

(33 citation statements)

References 84 publications

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“…Outer membrane proteins are good candidate for rational vaccine design and got much attention in recent times, as they are highly immunogenic, has lower adverse effect, plays major role in cell to cell communication, highly stable in elevated temperature and chemical treatments, induce specific antibodies, abundant localization and pathogenesis (Gerritzen, Martens, Wijffels, van der Pol, & Stork, 2017;Gu et al, 2018;Lin, Huang, & Zhang, 2002;Pan, Li, & Ye, 2016). For example, designing of epitope based peptide vaccine against Acinetobacter baumannii (Jahangiri, Rasooli, Owlia, Fooladi, & Salimian, 2017), Neisseria meningitidis serogroup B (Chandra, Singh, & Singh, 2010), S. Typhi (Verma et al, 2018), Vibrio cholerae (Rauta, Ashe, Nayak, & Nayak, 2016) has been proposed already. Although vaccine development based on epitope has become a popular notion, not much research has yet been performed in the event of iNTS.…”

Section: Discussionmentioning

confidence: 99%

In Silico Epitope-Based Peptide Vaccine Design against Invasive Non Typhoidal <em>Salmonella </em>(iNTS) Through Immunoinformatic Approaches

Ali¹,

Jahan²,

Khatun³

et al. 2020

Preprint

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Salmonella, especially invasive non-typhoidal Salmonella (iNTS) are responsible for developing various invasive diseases, and possess higher mortality rate, due to their higher antibiotic resistance profile than the other bacteria. Therefore, the present study was concerned to develop epitope based peptide vaccine against iNTS species as a successive and substitute protective measures. The study considered comprehensive Immunoinformatic approaches, followed by molecular docking and molecular dynamics simulation to predict the efficient vaccine candidate T cell and B cell epitopes, based on the outer membrane proteins. The study identified two best epitopes YGIFAITAL and KVLYGIFAI from total iNTS outer membrane proteins, which showed higher immunity, non-allergenicity, non-toxicity and also showed higher conservancy and population coverage values. Both epitopes showed higher binding affinity and stability towards HLA-C* 03:03. The MM-PBSA binding free energy showed the YGIFAITAL epitope binds more tightly with both MHC-I and MHC-II molecules. The total contact, H-bond analysis and RMSF results also validate the efficiency of these epitopes as vaccine candidate. The projected B cell epitopes AAPVQVGEAAGS, TGGGDGSNT and TGGGDGSNTGTTTT showed higher antigenicity. Overall, the study concluded that these epitopes can be considered as the potential vaccine candidate to make a successive vaccine against iNTS species. However, this result further needs to be validate by wet lab research to make successive vaccine with these projected epitopes.

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Section: Discussionmentioning

confidence: 99%

In Silico Epitope-Based Peptide Vaccine Design against Invasive Non Typhoidal <em>Salmonella </em>(iNTS) Through Immunoinformatic Approaches

Ali¹,

Jahan²,

Khatun³

et al. 2020

Preprint

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“…In recent years, with clarifying the native structure of AbOmpA, researchers have found that the amino acids of AbOmpA from a variety of clinical isolates are highly conserved (> 89%), while they are not homologous to human proteome [36]. By comparing various OmpA-like proteins, the two conservative amino acids, R286 and Asp271, which are located in C-terminal domain of OmpA, were identified.…”

Section: Ompa Structure and Functionmentioning

confidence: 99%

“…For example, a novel immunogenic model with 12 strands was obtained by modifying amino acid sequences of OmpA, in which K 320 and K 322 were substituted by Alanine, "NADEEFWN" was replaced by "YKYDFDGVNRGTRGTSEEGTL", "VVQPG QEAAAPAAAQ" located at C-terminal and position 1-24 of N-terminal were removed. This AbOmpA-derived antigen was capable of triggering the production of antibodies which kills Pseudomonas aeruginosa and A. baumannii [36]. Another way is to develop DNA vaccine, which has attracted more attention owing to the effectiveness and durability.…”

Section: Vaccinementioning

confidence: 99%

Outer membrane protein A (OmpA) as a potential therapeutic target for Acinetobacter baumannii infection

et al. 2020

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Acinetobacter baumannii (A. baumannii) is an important opportunistic pathogen causing serious nosocomial infections, which is considered as the most threatening Gram-negative bacteria (GNB). Outer membrane protein A (OmpA), a major component of outer membrane proteins (OMPs) in GNB, is a key virulence factor which mediates bacterial biofilm formation, eukaryotic cell infection, antibiotic resistance and immunomodulation. The characteristics of OmpA in Escherichia coli (E. coli) have been extensively studied since 1974, but only in recent years researchers started to clarify the functions of OmpA in A. baumannii. In this review, we summarized the structure and functions of OmpA in A. baumannii (AbOmpA), collected novel therapeutic strategies against it for treating A. baumannii infection, and emphasized the feasibility of using AbOmpA as a potential therapeutic target.

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“…Studies to reduce the host cell toxicity of recombinant A. baumannii revealed the importance of both N and C-terminal regions and the importance of lysine residues in NLS sequence. A synthetic OmpA with mutations at K320 and K322 to Alanine, replacing “NADEEFWN” sequence with “YKYDFDGVNRGTRGTSEEGTL” and deleting N-terminal signal sequence and “VVQPGQEAAAPAAAQ” at C-terminal resulted in least toxic but highly immunogenic OmpA ( Jahangiri et al, 2017 ). In addition to NLS, the N-terminal region of OmpA is bioinformatically predicted to be more immunogenic ( Darbandian and Sefid, 2016 ).…”

Section: Introductionmentioning

confidence: 99%

The Outer Membrane Proteins OmpA, CarO, and OprD of Acinetobacter baumannii Confer a Two-Pronged Defense in Facilitating Its Success as a Potent Human Pathogen

2020

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Of all the ESKAPE pathogens, carbapenem-resistant and multidrug-resistant Acinetobacter baumannii is the leading cause of hospital-acquired and ventilator-associated pneumonia. A. baumannii infections are notoriously hard to eradicate due to its propensity to rapidly acquire multitude of resistance determinants and the virulence factor cornucopia elucidated by the bacterium that help it fend off a wide range of adverse conditions imposed upon by host and environment. One such weapon in the arsenal of A. baumannii is the outer membrane protein (OMP) compendium. OMPs in A. baumannii play distinctive roles in facilitating the bacterial acclimatization to antibiotic- and host-induced stresses, albeit following entirely different mechanisms. OMPs are major immunogenic proteins in bacteria conferring bacteria host-fitness advantages including immune evasion, stress tolerance, and resistance to antibiotics and antibacterials. In this review, we summarize the current knowledge of major A. baumannii OMPs and discuss their versatile role in antibiotic resistance and virulence. Specifically, we explore how OmpA, CarO, and OprD-like porins mediate antibiotic and amino acid shuttle and host virulence.

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In silico design of an immunogen against Acinetobacter baumannii based on a novel model for native structure of Outer membrane protein A

Cited by 51 publications

References 84 publications

In Silico Epitope-Based Peptide Vaccine Design against Invasive Non Typhoidal <em>Salmonella </em>(iNTS) Through Immunoinformatic Approaches

In Silico Epitope-Based Peptide Vaccine Design against Invasive Non Typhoidal <em>Salmonella </em>(iNTS) Through Immunoinformatic Approaches

Outer membrane protein A (OmpA) as a potential therapeutic target for Acinetobacter baumannii infection

The Outer Membrane Proteins OmpA, CarO, and OprD of Acinetobacter baumannii Confer a Two-Pronged Defense in Facilitating Its Success as a Potent Human Pathogen

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