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 ◽  
...  
2014 ◽  
Vol 5 (2) ◽  
pp. 186-189 ◽  
Author(s):  
Sahana Vishwanath ◽  
Sandra Everett ◽  
Long Shen ◽  
Kishore Malyavantham ◽  
Lakshmanan Suresh ◽  
...  

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

2017 ◽  
Vol 18 (1) ◽  
pp. 25
Author(s):  
Mahful Septiawan ◽  
Budayatin Budayatin ◽  
Hidayat Teguh Wiyono ◽  
Kartika Senjarini

Although malaria had ever been virtually eradicated from Indonesia but currently malaria is recognized as a serious re-emerging threat to public health. This disease is caused by malaria parasite which is transmitted to human host by Anopheles mosquitoes as main vector. It has been widely observed that saliva of mosquito that transmits disease contains several factors that could enhance pathogen infection. Therefore, it should be possible to control pathogen transmission by vaccinating the host against the molecule(s) in saliva that potentiate the infection. However, immunogenic specific component in mosquitoes vectors of Malaria has not yet been identified so far. The objective of this study are to analyze protein profile of SDS-PAGE and to know the immunogity the protein extract of salivary gland from potential vector of Malaria i.e. An. aconitus We used immunogenic reaction between salivary gland extract of these vectors against pool of human sera which were collected from endemic area. The reaction conducted by the dot-blot analyze. SDS-PAGE studies showed 15 major polypeptide bands of 284, 100, 84, 75, 66, 57, 53, 48, 45, 38, 33, 29, 15, 14, and 11 kDa. The dot-blot studies showed that the protein extract of salivary gland from An. aconitus are immunogenic.


Author(s):  
Syubbanul Wathon ◽  
Fitria Mutiah ◽  
Rike Oktarianti ◽  
Kartika Senjarini

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.


EMBO Reports ◽  
2011 ◽  
Vol 12 (11) ◽  
pp. 1196-1203 ◽  
Author(s):  
Lei Liu ◽  
Sukanya Narasimhan ◽  
Jianfeng Dai ◽  
Lili Zhang ◽  
Gong Cheng ◽  
...  

2003 ◽  
Vol 31 (4) ◽  
pp. 801-805 ◽  
Author(s):  
E.E. LeClair

A cluster of related genes whose products show structural identity with bactericidal permeability-increasing protein (BPI) has been identified in the genomes of both mice (on chromosome 2) and humans (on chromosome 20). Genes in the cluster include those encoding parotid secretory protein (PSP), von Ebner minor salivary gland protein (VEMSGP) and sequences in the PLUNC (palate, lung and nasal epithelium clone) family, among others. This mini-review addresses the tissue-specific expression of these genes in the mouse.


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