Peptide Trends in Immunology and Infectious Diseases: Therapeutics, Diagnostics and (Bio)materials

A special issue of Vaccines (ISSN 2076-393X). This special issue belongs to the section "Clinical Immunology".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 13033

Special Issue Editor


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Guest Editor
Istituto di Scienze e Tecnologie Chimiche “Giulio Natta” (SCITEC), Consiglio Nazionale delle Ricerche, Via Alfonso Corti 12, 20133 Milano, Italy
Interests: bioactive peptides; peptide (nano)materials; peptide technologies for diagnostics
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Special Issue Information

Dear Colleagues,

It is a pleasure to invite your contribution to a Special Issue of Vaccines focusing on recent advances in peptide science for immunology and infectious diseases. In recent years, peptides have been in the spotlight due to several advantages, including unmatched chemical versatility and virtually unlimited possibilities for new application design. For example, peptides are currently being investigated in drug discovery programs, as valuable immune-reactive probes for diagnostics, in the development of novel biomaterials and biointerfaces, and as possible alternatives to full protein antigens in vaccination strategies. In this scenario, continuous innovations in peptide design, synthesis, and manipulation are driving peptide science towards unexplored advances in the years to come.

This Special Issue will collect recent breakthroughs in the use of peptides within the immunology and infectious diseases fields, highlighting their prominent relevance and showcasing future perspectives. Topics include but are not limited to innovative strategies for vaccine design and enhanced therapeutic efficacy, rational and computational design methodologies, novel biofunctionalization and bioconjugation methods, emerging diagnostic technologies, and peptide biomaterials. Scientists from various fields are, therefore, welcome to submit their contribution in the form of original research papers, review articles, short communications, and perspectives. Due to the current worldwide contingencies related to Covid-19, contributions covering new possibilities in this area are encouraged.

Dr. Alessandro Gori
Guest Editor

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

  • peptide vaccines
  • infectious diseases
  • peptide therapeutics
  • peptide diagnostics
  • peptide synthesis
  • biomaterials
  • bioconjugation strategies
  • drug design
  • drug discovery
  • Covid-19

Published Papers (4 papers)

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Research

11 pages, 1344 KiB  
Article
Identification of B-Cell Epitopes of HspA from Helicobacter pylori and Detection of Epitope Antibody Profiles in Naturally Infected Persons
by Xin Zhang, Shuli Sang, Qing Guan, Haoxia Tao, Yanchun Wang and Chunjie Liu
Vaccines 2022, 10(1), 65; https://0-doi-org.brum.beds.ac.uk/10.3390/vaccines10010065 - 31 Dec 2021
Cited by 1 | Viewed by 1262
Abstract
Helicobacter pylori (H. pylori), heat-shock protein A (HspA), is a bacterial heat-shock chaperone that serves as a nickel ion scavenging protein. Ni2+ is an important co-factor required for the maturation and enzymatic activity of H. pylori urease and [NiFe] hydrogenase, [...] Read more.
Helicobacter pylori (H. pylori), heat-shock protein A (HspA), is a bacterial heat-shock chaperone that serves as a nickel ion scavenging protein. Ni2+ is an important co-factor required for the maturation and enzymatic activity of H. pylori urease and [NiFe] hydrogenase, both of which are key virulence factors for pathogen survival and colonization. HspA is an important target molecule for the diagnosis, treatment, and immune prevention of H. pylori. In this work, HspA was truncated into five fragments to determine the location of an antigen immunodominant peptide. A series of overlapping, truncated 11-amino-acid peptides in immunodominant peptide fragments were synthesized chemically and screened by ELISA. The immunogenicity and antigenicity of the screened epitope peptides were verified by ELISA, Western blot, and lymphocyte proliferation tests. Two novel B-cell epitopes were identified, covering amino acids 2–31 of HspA, which are HP11 (2–12; KFQPLGERVLV) and HP19 (18–28; ENKTSSGIIIP). The antiserum obtained from HP11-KLH and HP19-KLH immunized mice can bind to naive HspA in H. pylori SS2000, rHspA expressed in E. coli, and the corresponding GST fusion peptide. Among HspA seropositive persons, the seropositive rates of HP11 and HP19 were 21.4% and 33.3%, respectively. Both of the B-cell epitopes of HspA are highly conserved epitopes with good antigenicity and immunogenicity. Full article
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13 pages, 1615 KiB  
Article
Identification of a Neutralizing Epitope on TOSV Gn Glycoprotein
by Claudia Gandolfo, Shibily Prathyumn, Chiara Terrosi, Gabriele Anichini, Gianni Gori Savellini, Davide Corti, Luisa Bracci, Antonio Lanzavecchia, Gleyder Roman-Sosa and Maria Grazia Cusi
Vaccines 2021, 9(8), 924; https://0-doi-org.brum.beds.ac.uk/10.3390/vaccines9080924 - 19 Aug 2021
Cited by 3 | Viewed by 2412
Abstract
Emerging and re-emerging viral infections have been an important public health problem in recent years. We focused our attention on Toscana virus (TOSV), an emergent neurotropic negative-strand RNA virus of the Phenuiviridae family. The mechanisms of protection against phlebovirus natural infection are not [...] Read more.
Emerging and re-emerging viral infections have been an important public health problem in recent years. We focused our attention on Toscana virus (TOSV), an emergent neurotropic negative-strand RNA virus of the Phenuiviridae family. The mechanisms of protection against phlebovirus natural infection are not known; however, it is supposed that a virus-neutralizing antibody response against viral glycoproteins would be useful to block the first stages of infection. By using an improved memory B cell immortalization method, we obtained a panel of human mAbs which reacted with TOSV antigens. We identified three epitopes of TOSV Gn glycoproteins by neutralizing mAbs using synthetic peptide arrays on membrane support (SPOT synthesis). These epitopes, separated in primary structure, might be exposed near one another as a conformational epitope in their native structure. In vivo studies were conducted to evaluate the humoral response elicited in mice immunized with the identified peptides. The results underlined the hypothesis that the first two peptides located in the NH2 terminus could form a conformational epitope, while the third, located near the transmembrane sequence in the carboxyl terminus, was necessary to strengthen neutralizing activity. Our results emphasize the importance of identifying neutralizing epitopes shared among the various phleboviruses, which could be exploited for the development of a potential epitope-based diagnostic assay or a polyvalent protective vaccine against different phleboviruses. Full article
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12 pages, 2044 KiB  
Article
Structure, Immunoreactivity, and In Silico Epitope Determination of SmSPI S. mansoni Serpin for Immunodiagnostic Application
by Stefano De Benedetti, Flavio Di Pisa, Enrico Mario Alessandro Fassi, Marina Cretich, Angelo Musicò, Roberto Frigerio, Alessandro Mussida, Mauro Bombaci, Renata Grifantini, Giorgio Colombo, Martino Bolognesi, Romualdo Grande, Nadia Zanchetta, Maria Rita Gismondo, Davide Mileto, Alessandro Mancon and Louise Jane Gourlay
Vaccines 2021, 9(4), 322; https://0-doi-org.brum.beds.ac.uk/10.3390/vaccines9040322 - 01 Apr 2021
Cited by 5 | Viewed by 2375
Abstract
The human parasitic disease Schistosomiasis is caused by the Schistosoma trematode flatworm that infects freshwaters in tropical regions of the world, particularly in Sub-Saharan Africa, South America, and the Far-East. It has also been observed as an emerging disease in Europe, due to [...] Read more.
The human parasitic disease Schistosomiasis is caused by the Schistosoma trematode flatworm that infects freshwaters in tropical regions of the world, particularly in Sub-Saharan Africa, South America, and the Far-East. It has also been observed as an emerging disease in Europe, due to increased immigration. In addition to improved therapeutic strategies, it is imperative to develop novel, rapid, and sensitive diagnostic tests that can detect the Schistosoma parasite, allowing timely treatment. Present diagnosis is difficult and involves microscopy-based detection of Schistosoma eggs in the feces. In this context, we present the 3.22 Å resolution crystal structure of the circulating antigen Serine protease inhibitor from S. mansoni (SmSPI), and we describe it as a potential serodiagnostic marker. Moreover, we identify three potential immunoreactive epitopes using in silico-based epitope mapping methods. Here, we confirm effective immune sera reactivity of the recombinant antigen, suggesting the further investigation of the protein and/or its predicted epitopes as serodiagnostic Schistosomiasis biomarkers. Full article
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11 pages, 2042 KiB  
Article
SARS-CoV-2 Epitope Mapping on Microarrays Highlights Strong Immune-Response to N Protein Region
by Angelo Musicò, Roberto Frigerio, Alessandro Mussida, Luisa Barzon, Alessandro Sinigaglia, Silvia Riccetti, Federico Gobbi, Chiara Piubelli, Greta Bergamaschi, Marcella Chiari, Alessandro Gori and Marina Cretich
Vaccines 2021, 9(1), 35; https://0-doi-org.brum.beds.ac.uk/10.3390/vaccines9010035 - 11 Jan 2021
Cited by 34 | Viewed by 6243
Abstract
A workflow for rapid SARS-CoV-2 epitope discovery on peptide microarrays is herein reported. The process started with a proteome-wide screening of immunoreactivity based on the use of a high-density microarray followed by a refinement and validation phase on a restricted panel of probes [...] Read more.
A workflow for rapid SARS-CoV-2 epitope discovery on peptide microarrays is herein reported. The process started with a proteome-wide screening of immunoreactivity based on the use of a high-density microarray followed by a refinement and validation phase on a restricted panel of probes using microarrays with tailored peptide immobilization through a click-based strategy. Progressively larger, independent cohorts of Covid-19 positive sera were tested in the refinement processes, leading to the identification of immunodominant regions on SARS-CoV-2 spike (S), nucleocapsid (N) protein and Orf1ab polyprotein. A summary study testing 50 serum samples highlighted an epitope of the N protein (region 155–71) providing good diagnostic performance in discriminating Covid-19 positive vs. healthy individuals. Using this epitope, 92% sensitivity and 100% specificity were reached for IgG detection in Covid-19 samples, and no cross-reactivity with common cold coronaviruses was detected. Likewise, IgM immunoreactivity in samples collected within the first month after symptoms onset showed discrimination ability. Overall, epitope 155–171 from N protein represents a promising candidate for further development and rapid implementation in serological tests. Full article
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