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Immunology and Vaccines Development on HIV, Measles, Chikungunya Virus and...
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Immunology and Vaccines Development on HIV, Measles, Chikungunya Virus and SARS-CoV-2

A special issue of Vaccines (ISSN 2076-393X). This special issue belongs to the section "Vaccines against Infectious Diseases".

Deadline for manuscript submissions: closed (30 August 2023) | Viewed by 2583

Special Issue Editors

Dr. Anil Kumar Verma

E-Mail Website
Guest Editor
Center for Immunology and Infectious Diseases, University of California Davis, 1 Shield Ave, Davis, CA 95616, USA
Interests: HIV immunology and vaccine development
Dr. Kaustuv Nayak

E-Mail Website1 Website2
Guest Editor
ICGEB-Emory Vaccine Center, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India
Interests: molecular virology; viral infection; viral immunology; virus cultivation; immunology of infectious diseases; vaccine development; cell culture

Special Issue Information

Dear Colleagues,

As commonly reported, HIV, measles, chikungunya virus, and SARS-CoV2 are global health issues. Recurrent productive infections are responsible for high morbidity and mortality. The induction of antigen/viral-specific immune responses plays an evident role in the development of a durable and effective vaccine. However, there is still an incomplete understanding of the immune response of pathways elicited by viral infections, fill gaps by the rational design of prophylactic and/or therapeutic vaccines, and the choice of the proper adjuvant to elicit protective response.

To achieve a more extensive understanding of recent scientific knowledge and current trends in viral vaccine development, this Special Issue focuses on the recent scientific and progresses made in this field. Based on your extensive knowledge and experience, we invite you to contribute an original report, original observation, or review to highlight (i) antibody protection, (ii) immune responses after primary/secondary infection, and (iii) recent advances in the development of novel prophylactic and therapeutic vaccines.

We look forward to receiving your contributions.

Dr. Anil Kumar Verma
Dr. Kaustuv Nayak
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Vaccines is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • T cell
  • antibody
  • immune responses
  • vaccine

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Published Papers (1 paper)

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Research

20 pages, 2917 KiB  
Article
Effect of Double Mutation (L452R and E484Q) on the Binding Affinity of Monoclonal Antibodies (mAbs) against the RBD—A Target for Vaccine Development
by Deepali Gupta, Mukesh Kumar, Priyanka Sharma, Trishala Mohan, Amresh Prakash, Renu Kumari and Punit Kaur
Vaccines 2023, 11(1), 23; https://doi.org/10.3390/vaccines11010023 - 22 Dec 2022
Cited by 5 | Viewed by 2174
Abstract
The COVID-19 pandemic, caused by SARS-CoV-2, emerges as a global health problem, as the viral genome is evolving rapidly to form several variants. Advancement and progress in the development of effective vaccines and neutralizing monoclonal antibodies are promising to combat viral infections. In [...] Read more.
The COVID-19 pandemic, caused by SARS-CoV-2, emerges as a global health problem, as the viral genome is evolving rapidly to form several variants. Advancement and progress in the development of effective vaccines and neutralizing monoclonal antibodies are promising to combat viral infections. In the current scenario, several lineages containing “co-mutations” in the receptor-binding domain (RBD) region of the spike (S) protein are imposing new challenges. Co-occurrence of some co-mutations includes delta (L452R/T478K), kappa (L452R/E484Q), and a common mutation in both beta and gamma variants (E484K/N501Y). The effect of co-mutants (L452R/E484Q) on human angiotensin-converting enzyme 2 (hACE2) binding has already been elucidated. Here, for the first time, we investigated the role of these RBD co-mutations (L452R/E484Q) on the binding affinity of mAbs by adopting molecular dynamics (MD) simulation and free-energy binding estimation. The results obtained from our study suggest that the structural and dynamic changes introduced by these co-mutations reduce the binding affinity of the viral S protein to monoclonal antibodies (mAbs). The structural changes imposed by L452R create a charged patch near the interfacial surface that alters the affinity towards mAbs. In E484Q mutation, polar negatively charged E484 helps in the formation of electrostatic interaction, while the neutrally charged Q residue affects the interaction by forming repulsive forces. MD simulations along with molecular mechanics-generalized Born surface area (MMGBSA) studies revealed that the REGN 10933, BD-368-2, and S2M11 complexes have reduced binding affinity towards the double-mutant RBD. This indicates that their mutant (MT) structures have a stronger ability to escape from most antibodies than the wild type (WT). However, EY6A Ab showed higher affinity towards the double MT-RBD complex as compared to the WT. However, no significant effect of the per-residue contribution of double-mutated residues was observed, as this mAb does not interact with the region harboring L452 and E484 residues. Full article
(This article belongs to the Special Issue Immunology and Vaccines Development on HIV, Measles, Chikungunya Virus and SARS-CoV-2)
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