Evaluation of a recombinant salivary gland protein (thrombostasin) as a vaccine candidate to disrupt blood-feeding by horn flies

Vaccine ◽  
2004 ◽  
Vol 22 (17-18) ◽  
pp. 2285-2297 ◽  
Author(s):  
Mary S Cupp ◽  
E.W Cupp ◽  
Christine Navarre ◽  
Nancy Wisnewski ◽  
Kevin S Brandt ◽  
...  
1995 ◽  
Vol 32 (3) ◽  
pp. 300-305 ◽  
Author(s):  
Claudia F. Golenda ◽  
Terry Klein ◽  
Russel Coleman ◽  
Robert Burge ◽  
Ronald A. Ward ◽  
...  

Author(s):  
Seena Kumari ◽  
Tanwee Das De ◽  
Charu Chauhan ◽  
Jyoti Rani ◽  
Sanjay Tevatiya ◽  
...  

AbstractIn the adult female mosquito, successful blood meal acquisition is accomplished by salivary glands, which releases a cocktail of proteins to counteract vertebrate host’s immune-homeostasis. However, the biological relevance of many salivary proteins remains unknown. Here, we characterize a salivary specific Heme peroxidase family member HPX12, originally identified from Plasmodium vivax infected salivary RNAseq data of the mosquito Anopheles stephensi. We demonstrate that dsRNA silencing mediated mRNA depletion of salivary AsHPX12 (80-90%), causes enhanced host attraction but reduced blood-meal acquisition abilities, by increasing probing propensity (31%), as well as probing time (100–200s, P<0.0001) as compared to control (35-90s) mosquitoes group. Altered expression of the salivary secretory and antennal proteins may account for an unusual fast release of salivary cocktail proteins, but the slowing acquisition of blood meal, possibly due to salivary homeostasis disruption of AsHPX12 silenced mosquitoes. A parallel transcriptional modulation in response to blood feeding and P. vivax infection, further establish a possible functional correlation of AsHPX12 role in salivary immune-physiology and Plasmodium sporozoites survival/transmission. We propose that salivary HPX12 may have a vital role in the management of ‘pre- and post’-blood meal associated physiological-homeostasis and parasite transmission.Graphical abstractFigure 1:Schematic representation of mosquito’s blood meal acquisition and upshot on blood-feeding after silencing of salivary gland HPX-12. (A) After landing over host skin, mosquito mouthparts (proboscis) actively engaged to search, probe, and pierce the skin followed by a rapid release of the pre-synthesized salivary cocktail, which counteracts the host homeostasis, inflammation, and immune responses, during blood meal uptake. (B) Silencing of HPX-12 disrupts salivary gland homeostasis, enhancing mosquito attraction, possibly by up-regulating odorant-binding proteins genes-OBP-7,10 and OBP-20 expression in the Olfactory System. However, HPX-12 disruption may also cause significant effects on pre-blood meal associated probing abilities, which may be due to fast down-regulation of salivary cocktail proteins such as Anopheline, Apyrase, D7L proteins.


2020 ◽  
Vol 58 (2) ◽  
pp. 161-171
Author(s):  
Qi Xiao ◽  
Yuhong Hu ◽  
Xiaohong Yang ◽  
Jianna Tang ◽  
Xiaoshuang Wang ◽  
...  

The ticks feed large amount of blood from their hosts and transmit pathogens to the victims. The salivary gland plays an important role in the blood feeding. When the female ticks are near engorgement, the salivary gland gradually loses its functions and begins to rapidly degenerate. In this study, data-independent acquisition quantitative proteomics was used to study changes in the phosphorylation modification of proteins during salivary gland degeneration in <i>Haemaphysalis longicornis</i>. In this quantitative study, 400 phosphorylated proteins and 850 phosphorylation modification sites were identified. Trough RNA interference experiments, we found that among the proteins with changes in phosphorylation, apoptosis-promoting Hippo protein played a role in salivary gland degeneration.


1992 ◽  
Vol 165 (1) ◽  
pp. 61-71 ◽  
Author(s):  
J. M. Ribeiro

Salivary gland homogenates and oil-induced saliva of the mosquito Aedes aegypti dilate the rabbit aortic ring and contract the guinea pig ileum. The vasodilatory activity is endothelium-dependent, heat-stable, sensitive to both trypsin and chymotrypsin treatments, and both smooth muscle activities cross-desensitize to the tachykinin peptide substance P. Both bioactivities co-elute when salivary gland homogenates are fractionated by reversed-phase HPLC. Molecular sieving chromatography indicates a relative molecular mass of 1400. A monoclonal antibody specific to the carboxy terminal region of tachykinins reacts with material in the posterior part of the central lobe of paraformaldehyde-fixed salivary glands. The presence of a vasodilatory peptide of the tachykinin family in the salivary glands of A. aegypti is proposed and its role in blood feeding is discussed.


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

1997 ◽  
Vol 48 (3) ◽  
pp. 211-218 ◽  
Author(s):  
Hiroyuki MATSUOKA ◽  
Hisashi MATSUBARA ◽  
Philomene WAIDHET ◽  
Tomoyuki HASHIMOTO ◽  
Akira ISHII ◽  
...  

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

2009 ◽  
Vol 46 (2) ◽  
pp. 351-357 ◽  
Author(s):  
Mary S. Cupp ◽  
Eddie W. Cupp ◽  
Dunhua Zhang ◽  
Xin Yue ◽  
Latora Todd ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document