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1.
Int J Mol Sci ; 22(17)2021 Aug 26.
Article in English | MEDLINE | ID: covidwho-1374425

ABSTRACT

Bifidobacteria are some of the major agents that shaped the immune system of many members of the animal kingdom during their evolution. Over recent years, the question of concrete mechanisms underlying the immunomodulatory properties of bifidobacteria has been addressed in both animal and human studies. A possible candidate for this role has been discovered recently. The PFNA cluster, consisting of five core genes, pkb2, fn3, aaa-atp, duf58, tgm, has been found in all gut-dwelling autochthonous bifidobacterial species of humans. The sensory region of the species-specific serine-threonine protein kinase (PKB2), the transmembrane region of the microbial transglutaminase (TGM), and the type-III fibronectin domain-containing protein (FN3) encoded by the I gene imply that the PFNA cluster might be implicated in the interaction between bacteria and the host immune system. Moreover, the FN3 protein encoded by one of the genes making up the PFNA cluster, contains domains and motifs of cytokine receptors capable of selectively binding TNF-α. The PFNA cluster could play an important role for sensing signals of the immune system. Among the practical implications of this finding is the creation of anti-inflammatory drugs aimed at alleviating cytokine storms, one of the dire consequences resulting from SARS-CoV-2 infection.


Subject(s)
Bacterial Proteins/genetics , Bifidobacterium/physiology , COVID-19/therapy , /genetics , Bacterial Proteins/chemistry , Bacterial Proteins/metabolism , COVID-19/immunology , COVID-19/virology , Cytokine Release Syndrome/immunology , Cytokine Release Syndrome/prevention & control , Cytokines/chemistry , Cytokines/metabolism , Humans , Immune System , Operon/genetics , /metabolism , SARS-CoV-2/isolation & purification
2.
FEBS Lett ; 595(18): 2323-2340, 2021 09.
Article in English | MEDLINE | ID: covidwho-1332924

ABSTRACT

The COVID-19 pandemic, caused by the SARS-CoV-2 coronavirus, has triggered a worldwide health emergency. Here, we show that ferritin-like Dps from hyperthermophilic Sulfolobus islandicus, covalently coupled with SARS-CoV-2 antigens via the SpyCatcher system, forms stable multivalent dodecameric vaccine nanoparticles that remain intact even after lyophilisation. Immunisation experiments in mice demonstrated that the SARS-CoV-2 receptor binding domain (RBD) coupled to Dps (RBD-S-Dps) elicited a higher antibody titre and an enhanced neutralising antibody response compared to monomeric RBD. A single immunisation with RBD-S-Dps completely protected hACE2-expressing mice from serious illness and led to viral clearance from the lungs upon SARS-CoV-2 infection. Our data highlight that multimerised SARS-CoV-2 subunit vaccines are a highly efficacious modality, particularly when combined with an ultra-stable scaffold.


Subject(s)
Angiotensin-Converting Enzyme 2/immunology , COVID-19 Vaccines/immunology , COVID-19/prevention & control , Receptors, Virus/immunology , Spike Glycoprotein, Coronavirus/immunology , Animals , Antibodies, Neutralizing/immunology , Antibodies, Viral/immunology , Bacterial Proteins/chemistry , COVID-19 Vaccines/administration & dosage , COVID-19 Vaccines/chemistry , DNA-Binding Proteins/chemistry , Ferritins/chemistry , Humans , Immunization , Mice , Nanoparticles , Protein Domains , Protein Multimerization , Spike Glycoprotein, Coronavirus/chemistry , Sulfolobus
3.
Int J Mol Sci ; 22(15)2021 Jul 27.
Article in English | MEDLINE | ID: covidwho-1332900

ABSTRACT

A novel series of N-substituted cis- and trans-3-aryl-4-(diethoxyphosphoryl)azetidin-2-ones were synthesized by the Kinugasa reaction of N-methyl- or N-benzyl-(diethyoxyphosphoryl)nitrone and selected aryl alkynes. Stereochemistry of diastereoisomeric adducts was established based on vicinal H3-H4 coupling constants in azetidin-2-one ring. All the obtained azetidin-2-ones were evaluated for the antiviral activity against a broad range of DNA and RNA viruses. Azetidin-2-one trans-11f showed moderate inhibitory activity against human coronavirus (229E) with EC50 = 45 µM. The other isomer cis-11f was active against influenza A virus H1N1 subtype (EC50 = 12 µM by visual CPE score; EC50 = 8.3 µM by TMS score; MCC > 100 µM, CC50 = 39.9 µM). Several azetidin-2-ones 10 and 11 were tested for their cytostatic activity toward nine cancerous cell lines and several of them appeared slightly active for Capan-1, Hap1 and HCT-116 cells values of IC50 in the range 14.5-97.9 µM. Compound trans-11f was identified as adjuvant of oxacillin with significant ability to enhance the efficacy of this antibiotic toward the highly resistant S. aureus strain HEMSA 5. Docking and molecular dynamics simulations showed that enantiomer (3R,4S)-11f can be responsible for the promising activity due to the potency in displacing oxacillin at ß-lactamase, thus protecting the antibiotic from undesirable biotransformation.


Subject(s)
Adjuvants, Pharmaceutic/chemistry , Adjuvants, Pharmaceutic/pharmacology , Antiviral Agents/chemistry , Antiviral Agents/pharmacology , Azetidines/pharmacology , Infections/drug therapy , Anti-Bacterial Agents/chemistry , Anti-Bacterial Agents/pharmacology , Azetidines/chemistry , Bacterial Proteins/chemistry , Cell Line, Tumor , Cell Proliferation/drug effects , Coronavirus 229E, Human/drug effects , Cytostatic Agents/chemistry , Cytostatic Agents/pharmacology , Humans , Influenza A Virus, H1N1 Subtype/drug effects , Molecular Dynamics Simulation , Oxacillin/chemistry , Penicillin-Binding Proteins/chemistry , Staphylococcus aureus/drug effects , Stereoisomerism , beta-Lactamases/chemistry
4.
PLoS One ; 16(7): e0254815, 2021.
Article in English | MEDLINE | ID: covidwho-1318322

ABSTRACT

African swine fever (ASF) is a serious contagious disease that causes fatal haemorrhagic fever in domestic and wild pigs, with high morbidity. It has caused devastating damage to the swine industry worldwide, necessitating the focus of attention on detection of the ASF pathogen, the African swine fever virus (ASFV). In order to overcome the disadvantages of conventional diagnostic methods (e.g. time-consuming, demanding and unintuitive), quick detection tools with higher sensitivity need to be explored. In this study, based on the conserved p72 gene sequence of ASFV, we combined the Cas12a-based assay with recombinase polymerase amplification (RPA) and a fluorophore-quencher (FQ)-labeled reporter assay for rapid and visible detection. Five crRNAs designed for Cas12a-based assay showed specificity with remarkable fluorescence intensity under visual inspection. Within 20 minutes, with an initial concentration of two copies of DNA, the assay can produce significant differences between experimental and negative groups, indicating the high sensitivity and rapidity of the method. Overall, the developed RPA-Cas12a-fluorescence assay provides a fast and visible tool for point-of-care ASFV detection with high sensitivity and specificity, which can be rapidly performed on-site under isothermal conditions, promising better control and prevention of ASF.


Subject(s)
African Swine Fever Virus/isolation & purification , African Swine Fever/diagnosis , Bacterial Proteins/genetics , CRISPR-Associated Proteins/genetics , Endodeoxyribonucleases/genetics , Swine Diseases/diagnosis , African Swine Fever/genetics , African Swine Fever/virology , African Swine Fever Virus/genetics , Animals , Bacterial Proteins/chemistry , CRISPR-Associated Proteins/chemistry , CRISPR-Cas Systems , DNA-Directed DNA Polymerase/chemistry , Endodeoxyribonucleases/chemistry , Molecular Diagnostic Techniques , Point-of-Care Systems , Recombinases/chemistry , Swine , Swine Diseases/genetics , Swine Diseases/pathology , Swine Diseases/virology
5.
Microbiology (Reading) ; 167(3)2021 03.
Article in English | MEDLINE | ID: covidwho-1288221

ABSTRACT

Biofilm formation in the human intestinal pathogen Vibrio cholerae is in part regulated by norspermidine, spermidine and spermine. V. cholerae senses these polyamines through a signalling pathway consisting of the periplasmic protein, NspS, and the integral membrane c-di-GMP phosphodiesterase MbaA. NspS and MbaA belong to a proposed class of novel signalling systems composed of periplasmic ligand-binding proteins and membrane-bound c-di-GMP phosphodiesterases containing both GGDEF and EAL domains. In this signal transduction pathway, NspS is hypothesized to interact with MbaA in the periplasm to regulate its phosphodiesterase activity. Polyamine binding to NspS likely alters this interaction, leading to the activation or inhibition of biofilm formation depending on the polyamine. The purpose of this study was to determine the amino acids important for NspS function. We performed random mutagenesis of the nspS gene, identified mutant clones deficient in biofilm formation, determined their responsiveness to norspermidine and mapped the location of these residues onto NspS homology models. Single mutants clustered on two lobes of the NspS model, but the majority were found on a single lobe that appeared to be more mobile upon norspermidine binding. We also identified residues in the putative ligand-binding site that may be important for norspermidine binding and interactions with MbaA. Ultimately, our results provide new insights into this novel signalling pathway in V. cholerae and highlight differences between periplasmic binding proteins involved in transport versus signal transduction.


Subject(s)
Bacterial Proteins/genetics , Biofilms , Vibrio cholerae/genetics , Amino Acid Sequence , Bacterial Proteins/chemistry , Bacterial Proteins/metabolism , Gene Expression Regulation, Bacterial , Mutagenesis , Periplasm/genetics , Periplasm/metabolism , Protein Domains , Sequence Alignment , Signal Transduction , Vibrio cholerae/chemistry , Vibrio cholerae/physiology
6.
Sci Rep ; 11(1): 12410, 2021 06 14.
Article in English | MEDLINE | ID: covidwho-1268005

ABSTRACT

In situ generation of antibacterial and antiviral agents by harnessing the catalytic activity of enzymes on surfaces provides an effective eco-friendly approach for disinfection. The perhydrolase (AcT) from Mycobacterium smegmatis catalyzes the perhydrolysis of acetate esters to generate the potent disinfectant, peracetic acid (PAA). In the presence of AcT and its two substrates, propylene glycol diacetate and H2O2, sufficient and continuous PAA is generated over an extended time to kill a wide range of bacteria with the enzyme dissolved in aqueous buffer. For extended self-disinfection, however, active and stable AcT bound onto or incorporated into a surface coating is necessary. In the current study, an active, stable and reusable AcT-based coating was developed by incorporating AcT into a polydopamine (PDA) matrix in a single step, thereby forming a biocatalytic composite onto a variety of surfaces. The resulting AcT-PDA composite coatings on glass, metal and epoxy surfaces yielded up to 7-log reduction of Gram-positive and Gram-negative bacteria when in contact with the biocatalytic coating. This composite coating also possessed potent antiviral activity, and dramatically reduced the infectivity of a SARS-CoV-2 pseudovirus within minutes. The single-step approach enables rapid and facile fabrication of enzyme-based disinfectant composite coatings with high activity and stability, which enables reuse following surface washing. As a result, this enzyme-polymer composite technique may serve as a general strategy for preparing antibacterial and antiviral surfaces for applications in health care and common infrastructure safety, such as in schools, the workplace, transportation, etc.


Subject(s)
Anti-Bacterial Agents/chemistry , Antiviral Agents/chemistry , Bacterial Proteins/chemistry , Hydrolases/chemistry , Indoles/chemistry , Polymers/chemistry , Anti-Bacterial Agents/metabolism , Anti-Bacterial Agents/pharmacology , Antiviral Agents/metabolism , Antiviral Agents/pharmacology , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , COVID-19/pathology , COVID-19/virology , Coated Materials, Biocompatible/chemistry , Coated Materials, Biocompatible/metabolism , Coated Materials, Biocompatible/pharmacology , Drug Stability , Gram-Negative Bacteria/drug effects , Gram-Positive Bacteria/drug effects , Humans , Hydrolases/genetics , Hydrolases/metabolism , Kinetics , Mycobacterium smegmatis/enzymology , Peracetic Acid/metabolism , Recombinant Proteins/biosynthesis , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification , SARS-CoV-2/drug effects
7.
Biochem Biophys Res Commun ; 558: 79-85, 2021 06 18.
Article in English | MEDLINE | ID: covidwho-1193239

ABSTRACT

During 2020, the COVID-19 pandemic affected almost 108 individuals. Quite a number of vaccines against COVID-19 were therefore developed, and a few recently received authorization for emergency use. Overall, these vaccines target specific viral proteins by antibodies whose synthesis is directly elicited or indirectly triggered by nucleic acids coding for the desired targets. Among these targets, the receptor binding domain (RBD) of COVID-19 spike protein (SP) does frequently occur in the repertoire of candidate vaccines. However, the immunogenicity of RBD per se is limited by its low molecular mass, and by a structural rearrangement of full-length SP accompanied by the detachment of RBD. Here we show that the RBD of COVID-19 SP can be conveniently produced in Escherichia coli when fused to a fragment of CRM197, a variant of diphtheria toxin currently used for a number of conjugated vaccines. In particular, we show that the CRM197-RBD chimera solubilized from inclusion bodies can be refolded and purified to a state featuring the 5 native disulphide bonds of the parental proteins, the competence in binding angiotensin-converting enzyme 2, and a satisfactory stability at room temperature. Accordingly, our observations provide compulsory information for the development of a candidate vaccine directed against COVID-19.


Subject(s)
Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Escherichia coli , Recombinant Fusion Proteins/biosynthesis , Recombinant Fusion Proteins/genetics , SARS-CoV-2 , Spike Glycoprotein, Coronavirus/chemistry , Spike Glycoprotein, Coronavirus/genetics , Bacterial Proteins/biosynthesis , Bacterial Proteins/isolation & purification , Base Sequence , COVID-19 Vaccines/chemistry , COVID-19 Vaccines/genetics , COVID-19 Vaccines/immunology , Escherichia coli/genetics , Escherichia coli/metabolism , Inclusion Bodies/chemistry , Inclusion Bodies/metabolism , Mass Spectrometry , Models, Molecular , Protein Refolding , Protein Stability , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/isolation & purification , SARS-CoV-2/chemistry , SARS-CoV-2/genetics , SARS-CoV-2/immunology , Spike Glycoprotein, Coronavirus/biosynthesis , Spike Glycoprotein, Coronavirus/isolation & purification , Temperature , Time Factors
8.
Biomolecules ; 11(3)2021 03 22.
Article in English | MEDLINE | ID: covidwho-1151739

ABSTRACT

Global processes, such as climate change, frequent and distant travelling and population growth, increase the risk of viral infection spread. Unfortunately, the number of effective and accessible medicines for the prevention and treatment of these infections is limited. Therefore, in recent years, efforts have been intensified to develop new antiviral medicines or vaccines. In this review article, the structure and activity of the most promising antiviral cyanobacterial products are presented. The antiviral cyanometabolites are mainly active against the human immunodeficiency virus (HIV) and other enveloped viruses such as herpes simplex virus (HSV), Ebola or the influenza viruses. The majority of the metabolites are classified as lectins, monomeric or dimeric proteins with unique amino acid sequences. They all show activity at the nanomolar range but differ in carbohydrate specificity and recognize a different epitope on high mannose oligosaccharides. The cyanobacterial lectins include cyanovirin-N (CV-N), scytovirin (SVN), microvirin (MVN), Microcystisviridis lectin (MVL), and Oscillatoria agardhii agglutinin (OAA). Cyanobacterial polysaccharides, peptides, and other metabolites also have potential to be used as antiviral drugs. The sulfated polysaccharide, calcium spirulan (CA-SP), inhibited infection by enveloped viruses, stimulated the immune system's response, and showed antitumor activity. Microginins, the linear peptides, inhibit angiotensin-converting enzyme (ACE), therefore, their use in the treatment of COVID-19 patients with injury of the ACE2 expressing organs is considered. In addition, many cyanobacterial extracts were revealed to have antiviral activities, but the active agents have not been identified. This fact provides a good basis for further studies on the therapeutic potential of these microorganisms.


Subject(s)
Antiviral Agents/chemistry , Cyanobacteria/chemistry , HIV/drug effects , Lectins/pharmacology , Polysaccharides/pharmacology , SARS-CoV-2/drug effects , Simplexvirus/drug effects , Anti-HIV Agents/pharmacology , Antineoplastic Agents/pharmacology , Antiviral Agents/pharmacology , Bacterial Proteins/chemistry , Bacterial Proteins/pharmacology , COVID-19/drug therapy , Carbohydrates/chemistry , Carbohydrates/pharmacology , Cyanobacteria/metabolism , HIV Infections/drug therapy , Humans , Lectins/chemistry , Lectins/metabolism , Polysaccharides/chemistry , Polysaccharides/metabolism
9.
mBio ; 12(2)2021 03 23.
Article in English | MEDLINE | ID: covidwho-1148106

ABSTRACT

Complement, contact activation, coagulation, and fibrinolysis are serum protein cascades that need strict regulation to maintain human health. Serum glycoprotein, a C1 inhibitor (C1-INH), is a key regulator (inhibitor) of serine proteases of all the above-mentioned pathways. Recently, an autotransporter protein, virulence-associated gene 8 (Vag8), produced by the whooping cough pathogen, Bordetella pertussis, was shown to bind to C1-INH and interfere with its function. Here, we present the structure of the Vag8-C1-INH complex determined using cryo-electron microscopy at a 3.6-Å resolution. The structure shows a unique mechanism of C1-INH inhibition not employed by other pathogens, where Vag8 sequesters the reactive center loop of C1-INH, preventing its interaction with the target proteases.IMPORTANCE The structure of a 10-kDa protein complex is one of the smallest to be determined using cryo-electron microscopy at high resolution. The structure reveals that C1-INH is sequestered in an inactivated state by burial of the reactive center loop in Vag8. By so doing, the bacterium is able to simultaneously perturb the many pathways regulated by C1-INH. Virulence mechanisms such as the one described here assume more importance given the emerging evidence about dysregulation of contact activation, coagulation, and fibrinolysis leading to COVID-19 pneumonia.


Subject(s)
Bacterial Proteins/metabolism , Bordetella pertussis/pathogenicity , Complement C1 Inhibitor Protein/metabolism , Immune Evasion , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Binding Sites , Blood Coagulation , Bordetella pertussis/chemistry , Bordetella pertussis/metabolism , Complement C1 Inhibitor Protein/chemistry , Complement System Proteins/metabolism , Cryoelectron Microscopy , Fibrinolysis , Models, Molecular , Mutation , Protein Binding , Protein Domains , Type V Secretion Systems/genetics , Type V Secretion Systems/metabolism , Virulence , Virulence Factors, Bordetella
10.
J Proteome Res ; 19(11): 4649-4654, 2020 11 06.
Article in English | MEDLINE | ID: covidwho-974860

ABSTRACT

The Bacillus Calmette-Guerin vaccine is still widely used in the developing world. The vaccination prevents infant death not only from tuberculosis but also from unrelated infectious agents, especially respiratory tract infections and neonatal sepsis. It is proposed that these off-target protective effects of the BCG vaccine are mediated by the general long-term boosting of innate immune mechanisms, also termed "trained innate immunity". Recent studies indicate that both COVID-19 incidence and total deaths are strongly associated with the presence or absence of national mandatory BCG vaccination programs and encourage the initiation of several clinical studies with the expectation that revaccination with BCG could reduce the incidence and severity of COVID-19. Here, presented results from the bioinformatics analysis of the Mycobacterium bovis (strain BCG/Pasteur 1173P2) proteome suggests four immunodominant antigens that could induce an immune response against SARS-CoV-2.


Subject(s)
BCG Vaccine , Bacterial Proteins , Betacoronavirus , Coronavirus Infections , Drug Repositioning , Pandemics , Pneumonia, Viral , BCG Vaccine/chemistry , BCG Vaccine/immunology , Bacterial Proteins/chemistry , Bacterial Proteins/immunology , Betacoronavirus/chemistry , Betacoronavirus/immunology , COVID-19 , COVID-19 Vaccines , Coronavirus Infections/immunology , Coronavirus Infections/prevention & control , Humans , Mycobacterium bovis/chemistry , Mycobacterium bovis/immunology , Pandemics/prevention & control , Pneumonia, Viral/immunology , Pneumonia, Viral/prevention & control , Proteome/chemistry , Proteome/immunology , SARS-CoV-2 , Viral Vaccines/chemistry , Viral Vaccines/immunology
11.
Immunity ; 53(6): 1315-1330.e9, 2020 12 15.
Article in English | MEDLINE | ID: covidwho-967948

ABSTRACT

Various vaccine strategies have been proposed in response to the global COVID-19 pandemic, each with unique strategies for eliciting immune responses. Here, we developed nanoparticle vaccines by covalently conjugating the self-assembled 24-mer ferritin to the receptor binding domain (RBD) and/or heptad repeat (HR) subunits of the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) spike (S) protein. Compared to monomer vaccines, nanoparticle vaccines elicited more robust neutralizing antibodies and cellular immune responses. RBD and RBD-HR nanoparticle vaccinated hACE2 transgenic mice vaccinated with RBD and/or RBD-HR nanoparticles exhibited reduced viral load in the lungs after SARS-CoV-2 challenge. RBD-HR nanoparticle vaccines also promoted neutralizing antibodies and cellular immune responses against other coronaviruses. The nanoparticle vaccination of rhesus macaques induced neutralizing antibodies, and T and B cell responses prior to boost immunization; these responses persisted for more than three months. RBD- and HR-based nanoparticles thus present a promising vaccination approach against SARS-CoV-2 and other coronaviruses.


Subject(s)
Bacterial Proteins/immunology , COVID-19 Vaccines/immunology , COVID-19/immunology , Ferritins/immunology , Helicobacter pylori/metabolism , Recombinant Fusion Proteins/immunology , SARS-CoV-2/physiology , Spike Glycoprotein, Coronavirus/immunology , Angiotensin-Converting Enzyme 2/genetics , Angiotensin-Converting Enzyme 2/metabolism , Animals , Antibodies, Neutralizing/metabolism , Antibodies, Viral/metabolism , Bacterial Proteins/chemistry , COVID-19 Vaccines/chemistry , Ferritins/chemistry , Humans , Macaca mulatta , Mice , Mice, Inbred BALB C , Nanoparticles/chemistry , Pandemics , Protein Binding , Spike Glycoprotein, Coronavirus/chemistry , Vaccination
12.
Nat Rev Mol Cell Biol ; 21(1): 1-2, 2020 01.
Article in English | MEDLINE | ID: covidwho-829678
13.
Med Hypotheses ; 144: 110030, 2020 Nov.
Article in English | MEDLINE | ID: covidwho-612684

ABSTRACT

Novel Coronavirus (SARS CoV-2), the etiological agent for the highly contagious Corona virus disease-2019 (COVID-19) pandemic has threatened global health and economy infecting around 5.8 million people and causing over 359,200 deaths (as of 28th May 2020, https://www.worldometers.info/coronavirus/). The clinical manifestations of infected patients generally range from asymptomatic or mild to severe illness, or even death. The ability of the virus to evade the host immune response have been major reasons for high morbidity and mortality. One of the important clinical observations under conditions of critical illness show increased risk of developing disseminated intravascular coagulation. Molecular mechanisms of how SARS CoV-2 induces such conditions still remain unclear. This report describes the presence of two unique motifs in the SARS CoV-2 nucleocapsid phosphoprotein (N-protein) that can potentially interact with fibrinogen and possibly prothrombin. This is based on an established function of secretory proteins in Staphylococcus aureus (S. aureus)-coagulase, Efb (Extracellular fibrinogen binding) and vWBP (von Willebrand factor Binding Protein), which are known to regulate the blood clotting cascade and the functions of host immune response. It is hypothesized that having protein interaction motifs that are homologous to these S. aureus proteins, the N-protein of this virus can mimic their functions, which may in turn play a crucial role in formation of blood clots in the host and help the virus evade host immune response. However, this hypothesis needs to be tested in vitro. Considering the overwhelming increase in the incidence of SARS CoV-2 infection globally, this information may be useful for further investigation and could help in deducing new therapeutic strategies to combat advanced stages of this disease.


Subject(s)
Bacterial Proteins/chemistry , COVID-19/virology , Coronavirus Nucleocapsid Proteins/chemistry , Fibrinogen/chemistry , Host-Pathogen Interactions/immunology , SARS-CoV-2 , Amino Acid Motifs , COVID-19/metabolism , Humans , Immune System , Models, Theoretical , Peptides/chemistry , Phosphoproteins/chemistry , Protein Binding , Protein Domains , Staphylococcus aureus/enzymology , von Willebrand Factor/chemistry
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