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Article ; Online: HtpG-A Major Virulence Factor and a Promising Vaccine Antigen against

Berisio, Rita / Barra, Giovanni / Napolitano, Valeria / Privitera, Mario / Romano, Maria / Squeglia, Flavia / Ruggiero, Alessia

Biomolecules

2024 Volume 14, Issue 4

Abstract: Tuberculosis (TB) is the leading global cause of death f rom an infectious bacterial agent. Therefore, limiting its epidemic spread is a pressing global health priority. The chaperone-like protein HtpG ... ...

Abstract	Tuberculosis (TB) is the leading global cause of death f rom an infectious bacterial agent. Therefore, limiting its epidemic spread is a pressing global health priority. The chaperone-like protein HtpG of
MeSH term(s)	Mycobacterium tuberculosis/immunology ; Antigens, Bacterial/immunology ; Antigens, Bacterial/chemistry ; Virulence Factors/immunology ; Virulence Factors/chemistry ; Humans ; Tuberculosis Vaccines/immunology ; Bacterial Proteins/immunology ; Bacterial Proteins/chemistry ; Tuberculosis/immunology ; Tuberculosis/prevention & control ; Tuberculosis/microbiology ; Animals ; Molecular Chaperones/immunology ; Molecular Chaperones/chemistry ; Molecular Chaperones/metabolism
Chemical Substances	Antigens, Bacterial ; Virulence Factors ; Tuberculosis Vaccines ; Bacterial Proteins ; Molecular Chaperones
Language	English
Publishing date	2024-04-11
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom14040471
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A Structural View at Vaccine Development against

Romano, Maria / Squeglia, Flavia / Kramarska, Eliza / Barra, Giovanni / Choi, Han-Gyu / Kim, Hwa-Jung / Ruggiero, Alessia / Berisio, Rita

Cells

2023 Volume 12, Issue 2

Abstract: Tuberculosis (TB) is still the leading global cause of death from an infectious bacterial agent. Limiting tuberculosis epidemic spread is therefore an urgent global public health priority. As stated by the WHO, to stop the spread of the disease we need a ...

Abstract	Tuberculosis (TB) is still the leading global cause of death from an infectious bacterial agent. Limiting tuberculosis epidemic spread is therefore an urgent global public health priority. As stated by the WHO, to stop the spread of the disease we need a new vaccine, with better coverage than the current
MeSH term(s)	Humans ; Mycobacterium tuberculosis ; Tuberculosis/prevention & control ; BCG Vaccine ; Tuberculosis Vaccines ; Vaccines, Subunit
Chemical Substances	BCG Vaccine ; Tuberculosis Vaccines ; Vaccines, Subunit
Language	English
Publishing date	2023-01-14
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells12020317
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Article ; Online: Structural and Biochemical Characterization of Endo-β-1,4-glucanase from Dictyoglomus thermophilum , a Hyperthermostable and Halotolerant Cellulase

Rita Berisio / Giovanni Barra / Maria Romano / Flavia Squeglia / Alessia Ruggiero

Catalysts, Vol 12, Iss 302, p

2022 Volume 302

Abstract: Enzymatic conversion of polysaccharides in the lignocellulosic biomass is currently the subject of intensive research and will be a key technology in future biorefineries. Using a bioinformatics approach, we previously identified a putative endo-β-1,4- ... ...

Abstract	Enzymatic conversion of polysaccharides in the lignocellulosic biomass is currently the subject of intensive research and will be a key technology in future biorefineries. Using a bioinformatics approach, we previously identified a putative endo-β-1,4-glucanase (DtCel5A) from Dictyoglomus thermophilum , a chemoorganotrophic and thermophilic bacterium. Here, we structurally and functionally characterize DtCel5A and show that it is endowed with remarkable thermal and chemical stability. The structural features of DtCel5A and of its complex with cellobiose have been investigated by combining X-ray crystallography and other biophysical studies. Importantly, biochemical assays show that DtCel5A retains its activity on cellulose at high temperatures and at elevated salt concentrations. These features make DtCel5A an enzyme with interesting biotechnological applications for biomass degradation.
Keywords	crystal structure ; thermostability ; endoglucanase ; enzyme ; cell wall ; Chemical technology ; TP1-1185 ; Chemistry ; QD1-999
Subject code	540
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Structural and Binding Properties of the Active Cell Wall Hydrolase RipA from M. tuberculosis, a Promising Biosensing Molecule for Early Warning Bacterial Detection.

Squeglia, Flavia / Marasco, Daniela / Ruggiero, Alessia / Testa, Genni / Esposito, Luciana / Berisio, Rita

Current medicinal chemistry

2022 Volume 29, Issue 24, Page(s) 4282–4292

Abstract: Background: Peptidoglycan is an essential component of the cell wall in all bacteria. In particular, the cell walls of Gram-positive bacteria are composed mostly of a thick layer of peptidoglycan. Its accessibility has important implications for their ... ...

Abstract	Background: Peptidoglycan is an essential component of the cell wall in all bacteria. In particular, the cell walls of Gram-positive bacteria are composed mostly of a thick layer of peptidoglycan. Its accessibility has important implications for their sensing in whole bacterial detection methodologies. Indeed, there is an urgent demand for rapid tests which can identify whole bacteria, e.g., directly at the point of care. Objective: The aim of this work is to explore the suitability of RipA, a key cell division protein of M. tuberculosis, for whole cell biosensing of Gram-positive bacteria. Methods: We here conducted Molecular Dynamics (MD) studies aimed at the understanding of the structural and dynamic features of active RipA and at the design of a suitable bioreceptor. Based on these studies, we engineered a RipA variant for covalent oriented immobilisation on golden surfaces and are able to bind peptidoglycan, albeit without degrading it. Surface Plasmon Resonance (SPR) was employed to check the ability of functionalized golden chips to recognize whole bacteria. Results: MD analyses elucidated the structural details of the active form of RipA and suggested that this enzyme, once inactivated, presents a rigid and well-exposed peptidoglycan recognition cleft. We engineered RipA for proper oriented immobilisation on golden chips for SPR studies. Results show that once chemically coupled to a golden chip, the developed RipA-based bioreceptor is able to detect B. subtilis, used as a model in a concentration-dependent mode. Conclusion: Results highlight the potential of the engineered molecule to be integrated in the development of early warning biosensors for Gram-positive contamination in clinical diagnosis or food-borne infections.
MeSH term(s)	Bacterial Proteins/metabolism ; Cell Wall/metabolism ; Endopeptidases/metabolism ; Hydrolases/metabolism ; Mycobacterium tuberculosis/metabolism ; Peptidoglycan/metabolism
Chemical Substances	Bacterial Proteins ; Peptidoglycan ; Hydrolases (EC 3.-) ; Endopeptidases (EC 3.4.-) ; RipA protein, Mycobacterium tuberculosis (EC 3.4.-)
Language	English
Publishing date	2022-02-07
Publishing country	United Arab Emirates
Document type	Journal Article
ZDB-ID	1319315-6
ISSN	1875-533X ; 0929-8673
ISSN (online)	1875-533X
ISSN	0929-8673
DOI	10.2174/0929867329666220203115122
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Article ; Online: Unveiling CD59-Antibody Interactions to Design Paratope-Mimicking Peptides for Complement Modulation.

Sandomenico, Annamaria / Ruggiero, Alessia / Iaccarino, Emanuela / Oliver, Angela / Squeglia, Flavia / Moreira, Miguel / Esposito, Luciana / Ruvo, Menotti / Berisio, Rita

International journal of molecular sciences

2023 Volume 24, Issue 10

Abstract: CD59 is an abundant immuno-regulatory human protein that protects cells from damage by inhibiting the complement system. CD59 inhibits the assembly of the Membrane Attack Complex (MAC), the bactericidal pore-forming toxin of the innate immune system. In ... ...

Abstract	CD59 is an abundant immuno-regulatory human protein that protects cells from damage by inhibiting the complement system. CD59 inhibits the assembly of the Membrane Attack Complex (MAC), the bactericidal pore-forming toxin of the innate immune system. In addition, several pathogenic viruses, including HIV-1, escape complement-mediated virolysis by incorporating this complement inhibitor in their own viral envelope. This makes human pathogenic viruses, such as HIV-1, not neutralised by the complement in human fluids. CD59 is also overexpressed in several cancer cells to resist the complement attack. Consistent with its importance as a therapeutical target, CD59-targeting antibodies have been proven to be successful in hindering HIV-1 growth and counteracting the effect of complement inhibition by specific cancer cells. In this work, we make use of bioinformatics and computational tools to identify CD59 interactions with blocking antibodies and to describe molecular details of the paratope-epitope interface. Based on this information, we design and produce paratope-mimicking bicyclic peptides able to target CD59. Our results set the basis for the development of antibody-mimicking small molecules targeting CD59 with potential therapeutic interest as complement activators.
MeSH term(s)	Humans ; Binding Sites, Antibody ; Complement System Proteins/metabolism ; CD59 Antigens/metabolism ; Complement Membrane Attack Complex/metabolism ; Complement Inactivating Agents ; HIV-1/physiology
Chemical Substances	Complement System Proteins (9007-36-7) ; CD59 Antigens ; Complement Membrane Attack Complex ; Complement Inactivating Agents ; CD59 protein, human (101754-01-2)
Language	English
Publishing date	2023-05-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24108561
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Article ; Online: Klebsiella

Maciejewska, Barbara / Squeglia, Flavia / Latka, Agnieszka / Privitera, Mario / Olejniczak, Sebastian / Switala, Paulina / Ruggiero, Alessia / Marasco, Daniela / Kramarska, Eliza / Drulis-Kawa, Zuzanna / Berisio, Rita

mBio

2023 Volume 14, Issue 5, Page(s) e0132923

Abstract: Importance: In this work, we determined the structure ... ...

Abstract	Importance: In this work, we determined the structure of
MeSH term(s)	Klebsiella/genetics ; Bacteriophages/genetics ; Klebsiella pneumoniae/genetics
Language	English
Publishing date	2023-09-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.01329-23
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Article: Structure based design of effective HtpG-derived vaccine antigens against

Ruggiero, Alessia / Choi, Han-Gyu / Barra, Giovanni / Squeglia, Flavia / Back, Young Woo / Kim, Hwa-Jung / Berisio, Rita

Frontiers in molecular biosciences

2022 Volume 9, Page(s) 964645

Abstract: Vaccine development against Tuberculosis is a strong need, given the low efficacy of the sole vaccine hitherto used, the Bacillus Calmette-Guérin (BCG) vaccine. The chaperone-like protein ... ...

Abstract	Vaccine development against Tuberculosis is a strong need, given the low efficacy of the sole vaccine hitherto used, the Bacillus Calmette-Guérin (BCG) vaccine. The chaperone-like protein HtpG
Language	English
Publishing date	2022-08-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2022.964645
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Article: The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial Cytokinesis: A Structural Perspective.

Squeglia, Flavia / Moreira, Miguel / Ruggiero, Alessia / Berisio, Rita

Cells

2019 Volume 8, Issue 6

Abstract: In preparation for division, bacteria replicate their DNA and segregate the newly formed chromosomes. A division septum then assembles between the chromosomes, and the mother cell splits into two identical daughters due to septum degradation. A major ... ...

Abstract	In preparation for division, bacteria replicate their DNA and segregate the newly formed chromosomes. A division septum then assembles between the chromosomes, and the mother cell splits into two identical daughters due to septum degradation. A major constituent of bacterial septa and of the whole cell wall is peptidoglycan (PGN), an essential cell wall polymer, formed by glycan chains of β-(1-4)-linked-
MeSH term(s)	Acetylglucosamine/metabolism ; Amino Acid Sequence ; Bacterial Proteins/metabolism ; Bacterial Proteins/physiology ; Cell Division ; Cell Wall/metabolism ; Crystallography, X-Ray ; Cytokinesis/physiology ; Endopeptidases/metabolism ; Hydrolysis ; Lipoproteins/metabolism ; Lipoproteins/physiology ; Models, Molecular ; Muramic Acids/metabolism ; Mycobacterium/enzymology ; Mycobacterium/metabolism ; Mycobacterium tuberculosis/enzymology ; Mycobacterium tuberculosis/metabolism ; N-Acetylmuramoyl-L-alanine Amidase/chemistry ; Peptidoglycan/genetics ; Protein Conformation
Chemical Substances	Bacterial Proteins ; Lipoproteins ; Muramic Acids ; P60 protein, bacteria ; Peptidoglycan ; N-acetylmuramic acid (246FXU111L) ; Endopeptidases (EC 3.4.-) ; N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2019-06-18
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409
ISSN	2073-4409
DOI	10.3390/cells8060609
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: PE_PGRS33, an Important Virulence Factor of

Kramarska, Eliza / Squeglia, Flavia / De Maio, Flavio / Delogu, Giovanni / Berisio, Rita

Cells

2021 Volume 10, Issue 1

Abstract: PE_PGRS proteins are surface antigens ... ...

Abstract	PE_PGRS proteins are surface antigens of
MeSH term(s)	Alleles ; Animals ; Antigens/chemistry ; Antigens, Bacterial/immunology ; Antigens, Surface/metabolism ; Bacterial Proteins/immunology ; Cell Wall/metabolism ; Humans ; Immune System ; Immunity, Humoral ; Macrophages/metabolism ; Membrane Proteins/immunology ; Mycobacterium tuberculosis/immunology ; Protein Domains ; Surface Properties ; Toll-Like Receptor 2/metabolism ; Tuberculosis/immunology ; Tuberculosis/prevention & control ; Tuberculosis Vaccines/therapeutic use ; Virulence Factors/immunology
Chemical Substances	Antigens ; Antigens, Bacterial ; Antigens, Surface ; Bacterial Proteins ; Membrane Proteins ; PE-PGRS protein, Mycobacterium ; TLR2 protein, human ; Toll-Like Receptor 2 ; Tuberculosis Vaccines ; Virulence Factors
Language	English
Publishing date	2021-01-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10010161
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins.

Squeglia, Flavia / Romano, Maria / Ruggiero, Alessia / Maga, Giovanni / Berisio, Rita

Frontiers in chemistry

2020 Volume 8, Page(s) 602162

Abstract: As intracellular parasites, viruses hijack the host cell metabolic machinery for their replication. Among other cellular proteins, the DEAD-box (DDX) RNA helicases have been shown to be hijacked by coronaviruses and to participate in essential DDX- ... ...

Abstract	As intracellular parasites, viruses hijack the host cell metabolic machinery for their replication. Among other cellular proteins, the DEAD-box (DDX) RNA helicases have been shown to be hijacked by coronaviruses and to participate in essential DDX-mediated viral replication steps. Human DDX RNA helicases play essential roles in a broad array of biological processes and serve multiple roles at the virus-host interface. The viral proteins responsible for DDX interactions are highly conserved among coronaviruses, suggesting that they might also play conserved functions in the SARS-CoV-2 replication cycle. In this review, we provide an update of the structural and functional data of DDX as possible key factors involved in SARS-CoV-2 hijacking mechanisms. We also attempt to fill the existing gaps in the available structural information through homology modeling. Based on this information, we propose possible paths exploited by the virus to replicate more efficiently by taking advantage of host DDX proteins. As a general rule, sequestration of DDX helicases by SARS-CoV-2 is expected to play a pro-viral role in two ways: by enhancing key steps of the virus life cycle and, at the same time, by suppressing the host innate immune response.
Language	English
Publishing date	2020-12-10
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2711776-5
ISSN	2296-2646
ISSN	2296-2646
DOI	10.3389/fchem.2020.602162
Database	MEDical Literature Analysis and Retrieval System OnLINE

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