scholarly journals Profiling Autoantibodies against Salivary Proteins in Sicca Conditions

2019 ◽  
Vol 98 (7) ◽  
pp. 772-778 ◽  
Author(s):  
P.D. Burbelo ◽  
E.M.N. Ferré ◽  
A. Chaturvedi ◽  
J.A. Chiorini ◽  
I. Alevizos ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Salivary Protein ◽  
Sudden Onset ◽  
Small Subset ◽  
Inflammatory Infiltration ◽  
Protein Targets ◽  
Additional Testing ◽  
Salivary Gland Protein ◽  
Oral Dryness ◽  
Humoral Responses

Salivary gland dysfunction occurs in several autoimmune and immune-related conditions, including Sjögren syndrome (SS); immune checkpoint inhibitor-induced sicca (ICIS) that develops in some cancer patients and is characterized by severe, sudden-onset dry mouth; and autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED). Although subjects with these conditions present with oral dryness and often exhibit inflammatory infiltration of the salivary gland, little is known about the B-cell humoral responses directed against salivary gland protein targets. In this study, autoantibodies were evaluated against Ro52, Ro60, and La, as well as against a panel of 22 proteins derived from the salivary proteome. The tested cohort included healthy volunteers and subjects with SS, ICIS, and APECED without and with sicca. As expected, a high percentage of autoantibody seropositivity was detected against Ro52, Ro60, and La in SS, but only a few ICIS patients were seropositive for these autoantigens. A few APECED subjects also harbored autoantibodies to Ro52 and La, but only Ro60 autoantibodies were weakly associated with a small subset of APECED patients with sicca. Additional testing of the salivary panel failed to detect seropositive autoantibodies against any of the salivary-enriched proteins in the SS and ICIS subjects. However, APECED subjects selectively demonstrated seropositivity against BPI fold containing family A member 1 (BPIFA1), BPI fold containing family A member 2 (BPIFA2)/parotid salivary protein (PSP), and lactoperoxidase, 3 salivary-enriched proteins. Moreover, high levels of serum autoantibodies against BPIFA1 and BPIFA2/PSP occurred in 30% and 67% of the APECED patients with sicca symptoms, respectively, and were associated with an earlier age onset of oral dryness ( P = 0.001). These findings highlight the complexity of humoral responses in different sicca diseases and provide new insights and biomarkers for APECED-associated sicca (ClinicalTrials.gov: NCT00001196; NCT00001390; NCT01425892; NCT01386437).

Depletion of Total Salivary Gland Protein in Blood-Fed Anopheles Mosquitoes

1995 ◽  
Vol 32 (3) ◽  
pp. 300-305 ◽  
Author(s):  
Claudia F. Golenda ◽  
Terry Klein ◽  
Russel Coleman ◽  
Robert Burge ◽  
Ronald A. Ward ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Anopheles Mosquitoes ◽  
Salivary Gland Protein

scholarly journals Xerophthalmia of Sjogren's Syndrome Diagnosed with Anti-Salivary Gland Protein 1 Antibodies

2014 ◽  
Vol 5 (2) ◽  
pp. 186-189 ◽  
Author(s):  
Sahana Vishwanath ◽  
Sandra Everett ◽  
Long Shen ◽  
Kishore Malyavantham ◽  
Lakshmanan Suresh ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Sjögren’S Syndrome ◽  
Sjögren's Syndrome ◽  
Sjogren’S Syndrome ◽  
Sjogren's Syndrome ◽  
Salivary Gland Protein ◽  
Sjögren‘S Syndrome

scholarly journals A systematic review of methods to diagnose oral dryness and salivary gland function

2012 ◽  
Vol 12 (1) ◽  
Author(s):  
Christina Diogo Löfgren ◽  
Claes Wickström ◽  
Mikael Sonesson ◽  
Pablo Tapia Lagunas ◽  
Cecilia Christersson
Keyword(s):  
Systematic Review ◽  
Salivary Gland ◽  
Salivary Gland Function ◽  
Oral Dryness ◽  
Gland Function

Oral Signs and Symptoms as Predictors of Salivary Gland Hypofunction in General Dental Practice

2001 ◽  
Vol os8 (3) ◽  
pp. 111-114 ◽  
Author(s):  
E Anne Field ◽  
Lesley P Longman ◽  
Simon Fear ◽  
Susan Higham ◽  
Jocelyne Rostron ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Oral Mucosa ◽  
Clinical Signs ◽  
Signs And Symptoms ◽  
Dental Practice ◽  
General Dental Practice ◽  
Objective Evidence ◽  
Oral Dryness ◽  
Dental Practices ◽  
Salivary Gland Hypofunction

Objective To evaluate the signs and symptoms of oral dryness as predictors of salivary gland hypofunction (SGH) in general dental practice. Design and setting Prospective study recruiting adult patients attending five general dental practices in Merseyside in 1999. Materials and method Patients were screened for subjective symptoms of oral dysfunction and clinical signs of oral dryness. Patients with oral symptoms or signs of SGH were invited to undergo sialometry. Results were analysed using multiple logistic regression. Results 1103 patients were screened for signs and symptoms of oral dryness, 115 reported continuous xerostomia, of these 65 were also clinically (subjectively) assessed as having a dry oral mucosa. One hundred and one patients attended for sialometry and 73% of these had objective evidence of SGH. Neither the patients’ complaints of oral dryness or the assessment of dryness of the oral mucosa were significant predictors of SGH. Conclusions Symptoms of oral dysfunction and clinical signs of oral dryness were not significant predictors of SGH in dental practice.

scholarly journals A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation

Blood ◽  
2011 ◽  
Vol 117 (2) ◽  
pp. 736-744 ◽  
Author(s):  
Jindrich Chmelar ◽  
Carlo J. Oliveira ◽  
Pavlina Rezacova ◽  
Ivo M. B. Francischetti ◽  
Zuzana Kovarova ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Serine Proteases ◽  
Acute Inflammation ◽  
Biological Activities ◽  
Salivary Protein ◽  
Cathepsin G ◽  
Skin Injury ◽  
Edema Formation ◽  
Protein Targets ◽  
First Time

Abstract Platelet aggregation and acute inflammation are key processes in vertebrate defense to a skin injury. Recent studies uncovered the mediation of 2 serine proteases, cathepsin G and chymase, in both mechanisms. Working with a mouse model of acute inflammation, we revealed that an exogenous salivary protein of Ixodes ricinus, the vector of Lyme disease pathogens in Europe, extensively inhibits edema formation and influx of neutrophils in the inflamed tissue. We named this tick salivary gland secreted effector as I ricinus serpin-2 (IRS-2), and we show that it primarily inhibits cathepsin G and chymase, while in higher molar excess, it affects thrombin activity as well. The inhibitory specificity was explained using the crystal structure, determined at a resolution of 1.8 Å. Moreover, we disclosed the ability of IRS-2 to inhibit cathepsin G-induced and thrombin-induced platelet aggregation. For the first time, an ectoparasite protein is shown to exhibit such pharmacological effects and target specificity. The stringent specificity and biological activities of IRS-2 combined with the knowledge of its structure can be the basis for the development of future pharmaceutical applications.

Tick derived salivary gland protein IRAC 1 and IRAC 2

2007 ◽  
Vol 44 (16) ◽  
pp. 3991-3992
Author(s):  
Michael Reuter ◽  
Alain Vanderplaschen ◽  
Peter Kraiczy ◽  
Christine Skerka ◽  
Peter F. Zipfel
Keyword(s):  
Salivary Gland ◽  
Salivary Gland Protein

scholarly journals PURIFIKASI PROTEIN IMUNOGENIK 31 DAN 56 kDa DARI KELENJAR SALIVA Aedes aegypti

2020 ◽  
Vol 7 (1) ◽  
Author(s):  
Syubbanul Wathon ◽  
Fitria Mutiah ◽  
Rike Oktarianti ◽  
Kartika Senjarini
Keyword(s):  
Salivary Gland ◽  
Aedes Aegypti ◽  
Positive Control ◽  
Protein Fractions ◽  
Immunogenic Protein ◽  
Dot Blot ◽  
Molecular Weights ◽  
Sds Page ◽  
Salivary Gland Protein ◽  
Immunogenic Proteins

Purification of 31 and 56 kDa Immunogenic Proteins from the Salivary Glands of Aedes aegyptiThe salivary gland of arthropod vector contains various bioactive compounds and plays a role in the transmission of pathogens to the host. The host develops anti-salivary antibodies against vector saliva exposure. Our previous research has identified two immunogenic proteins with molecular weights of 31 and 56 kDa from the Aedes aegypti salivary gland protein extract. However, the role of the 31 and 56 kDa immunogenic proteins from saliva Ae. aegypti is not fully known, so it is necessary to purify two immunogenic protein fractions to better specify the target of developing a dengue vaccine. This study aimed to purify the 31 and 56 kDa immunogenic protein fractions by electroelution and dialysis methods. The purification of the two protein fractions has been successful which were confirmed by the SDS-PAGE by the existence of single-band parallel to the positive control. These results were further supported by the dot blot analysis which showed a positive reaction in the form of dark spots in the two protein fractions which were reacted with dengue patients' serum, endemic healthy people, and neonates. These results indicated that the purified 31 and 56 kDa immunogenic protein fraction can be identified by specific antibodies.Keywords: dialysis, electroelution, immunogenic, purification, saliva  ABSTRAKKelenjar saliva vektor arthropoda mengandung berbagai senyawa bioaktif dan berperan dalam transmisi patogen ke tubuh inang. Tubuh inang mengembangkan antibodi anti-saliva terhadap paparan saliva vektor. Penelitian kami sebelumnya telah mengidentifikasi dua protein imunogenik dengan berat molekul 31 dan 56 kDa dari ekstrak protein kelenjar saliva Aedes aegypti. Namun demikian, peranan protein imunogenik 31 dan 56 kDa dari saliva Ae. aegypti belum diketahui sepenuhnya sehingga perlu dilakukan purifikasi dua fraksi protein imunogenik untuk lebih menspesifikkan target pengembangan vaksin dengue. Tujuan penelitian ini untuk melakukan purifikasi fraksi protein imunogenik 31 dan 56 kDa melalui metode elektroelusi dan dialisis. Keberhasilan purifikasi dua fraksi protein 31 dan 56 kDa terbukti dari hasil konfirmasi SDS-PAGE dengan terbentuknya pita tunggal sejajar dengan kontrol positif. Hasil tersebut diperkuat dengan analisis dot blot yang menunjukkan reaksi positif dengan munculnya noktah gelap pada dua fraksi protein tersebut ketika direaksikan dengan serum pasien DBD, penduduk sehat endemik dan neonatus. Hasil ini mengindikasikan bahwa fraksi protein imunogenik 31 dan 56 kDa hasil purifikasi dapat dikenali oleh antibodi spesifik.

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