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1.
Arch Razi Inst ; 77(5): 1587-1591, 2022 10.
Article in English | MEDLINE | ID: covidwho-1939566

ABSTRACT

Saliva is one of the most significant components in maintaining oral homeostasis and symbiosis. It contains antimicrobial proteins and peptides, such as mucins, lactoferrin, lysozyme, lactoperoxidase, Catherine, statins, and antibodies (secretory immunoglobin A [sIgA]). Early defenses against respiratory infections rely heavily on mucosal immunity, especially secretory sIgA, which has several features and functions that make it suitable for mucosal defense. Salivary testing has been utilized to define mucosal immune responses to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Lysozyme has muramidase, with antimicrobial activity, and high concentrations in body fluids, such as saliva and tear. This research aimed to offer an update on how saliva components suppress viral infection and sustain health. A total of 50 individuals, including 30 SARS-2 patients and 20 non-infected subjects, in the age range of 32-54 years were enrolled in this study. Saliva specimens were obtained from polymerase chain reaction (PCR)-confirmed coronavirus disease 2019 (COVID-19) patients and non-infected participants. To collect saliva, the subjects were advised to swirl water over their lips three times, and 5.0 ml of saliva was collected. Samples were centrifuged at 800 x g for 10 min. Saliva was diluted at 1:2,000 with 1 × Diluent N. The immunoglobulin A (IgA) titer in saliva was detected. A spectrophotometer was used to measure the solution's change in absorbance at 550 nm. Measurements (salivary IgA and lysozyme) were made after 7, 30, and 60 days of confirmatory PCR COVID-19 test. The mean scores of salivary IgA levels were obtained at 17.85, 15.26, and 10.73 mg/dl in patients and 9.53, 10.33, and 9.21 mg/dl in healthy individuals after 7, 30, and 60 days, respectively. The salivary lysozyme activity levels in SARS-2 patients compared to controls were 9.7, 7.3, and 4.2 mg/dl versus 2.9, 3.4, and 3.77 mg/dl, respectively. The salivary IgA level was significantly higher in patients of a confirmatory test for COVID-19 compared to healthy individuals.


Subject(s)
Anti-Infective Agents , COVID-19 , Saliva , Anti-Infective Agents/metabolism , COVID-19/diagnosis , Immunoglobulin A/metabolism , Immunoglobulin A, Secretory/analysis , Immunoglobulin A, Secretory/metabolism , Iraq , Muramidase/analysis , Muramidase/metabolism , SARS-CoV-2 , Humans , Male , Female , Adult , Middle Aged , Saliva/virology
2.
PLoS One ; 17(2): e0263419, 2022.
Article in English | MEDLINE | ID: covidwho-1674014

ABSTRACT

Mucosal immunity plays a crucial role in controlling upper respiratory infections, including influenza. We established a quantitative ELISA to measure the amount of influenza virus-specific salivery IgA (sIgA) and salivary IgG (sIgG) antibodies using a standard antibody broadly reactive to the influenza A virus. We then analyzed saliva and serum samples from seven individuals infected with the A(H1N1)pdm09 influenza virus during the 2019-2020 flu seasons. We detected an early (6-10 days post-infection) increase of sIgA in five of the seven samples and a later (3-5 weeks) increase of sIgG in six of the seven saliva samples. Although the conventional parenteral influenza vaccine did not induce IgA production in saliva, vaccinated individuals with a history of influenza infection had higher basal levels of sIgA than those without a history. Interestingly, we observed sIgA and sIgG in an asymptomatic individual who had close contact with two influenza cases. Both early mucosal sIgA secretion and late systemically induced sIgG in the mucosal surface may protect against virus infection. Despite the small sample size, our results indicate that the saliva test system can be useful for analyzing upper mucosal immunity in influenza.


Subject(s)
Immunity, Mucosal/physiology , Influenza, Human/immunology , Saliva/immunology , Adult , Aged , Antibodies, Viral/analysis , Antibodies, Viral/metabolism , Antibody Formation , Cohort Studies , Female , History, 21st Century , Humans , Immunoglobulin A/analysis , Immunoglobulin A/metabolism , Immunoglobulin A, Secretory/analysis , Immunoglobulin A, Secretory/metabolism , Immunoglobulin G/analysis , Immunoglobulin G/metabolism , Influenza A Virus, H1N1 Subtype/immunology , Influenza Vaccines/therapeutic use , Influenza, Human/diagnosis , Influenza, Human/prevention & control , Japan , Longitudinal Studies , Male , Predictive Value of Tests , Prognosis , Saliva/chemistry , Saliva/metabolism , Young Adult
3.
Nat Commun ; 11(1): 4198, 2020 08 21.
Article in English | MEDLINE | ID: covidwho-724360

ABSTRACT

COVID-19 caused by SARS-CoV-2 has become a global pandemic requiring the development of interventions for the prevention or treatment to curtail mortality and morbidity. No vaccine to boost mucosal immunity, or as a therapeutic, has yet been developed to SARS-CoV-2. In this study, we discover and characterize a cross-reactive human IgA monoclonal antibody, MAb362. MAb362 binds to both SARS-CoV and SARS-CoV-2 spike proteins and competitively blocks ACE2 receptor binding, by overlapping the ACE2 structural binding epitope. Furthermore, MAb362 IgA neutralizes both pseudotyped SARS-CoV and SARS-CoV-2 in 293 cells expressing ACE2. When converted to secretory IgA, MAb326 also neutralizes authentic SARS-CoV-2 virus while the IgG isotype shows no neutralization. Our results suggest that SARS-CoV-2 specific IgA antibodies, such as MAb362, may provide effective immunity against SARS-CoV-2 by inducing mucosal immunity within the respiratory system, a potentially critical feature of an effective vaccine.


Subject(s)
Antibodies, Monoclonal/immunology , Antibodies, Neutralizing/immunology , Betacoronavirus/immunology , Immunoglobulin A/immunology , Peptidyl-Dipeptidase A/metabolism , Spike Glycoprotein, Coronavirus/metabolism , Angiotensin-Converting Enzyme 2 , Animals , Antibodies, Monoclonal/metabolism , Antibodies, Neutralizing/metabolism , Chlorocebus aethiops , Cross Reactions , Epitopes , HEK293 Cells , Humans , Immunoglobulin A/metabolism , Immunoglobulin A, Secretory/immunology , Immunoglobulin A, Secretory/metabolism , Immunoglobulin G/immunology , Immunoglobulin G/metabolism , Models, Molecular , Mutation , Protein Binding , Protein Interaction Domains and Motifs , Severe acute respiratory syndrome-related coronavirus/immunology , SARS-CoV-2 , Spike Glycoprotein, Coronavirus/chemistry , Spike Glycoprotein, Coronavirus/genetics , Spike Glycoprotein, Coronavirus/immunology , Vero Cells
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