title: Infection by chikungunya virus modulates the expression of several proteins in Aedes aegypti salivary glands.
abstract: BACKGROUND
  Arthropod-borne viral infections cause several emerging and resurging infectious diseases. Among the diseases caused by arboviruses, chikungunya is responsible for a high level of severe human disease worldwide. The salivary glands of mosquitoes are the last barrier before pathogen transmission.
  
  
  METHODS
  We undertook a proteomic approach to characterize the key virus/vector interactions and host protein modifications that occur in the salivary glands that could be responsible for viral transmission by using quantitative two-dimensional electrophoresis.
  
  
  RESULTS
  We defined the protein modulations in the salivary glands of Aedes aegypti that were triggered 3 and 5 days after an oral infection (3 and 5 DPI) with chikungunya virus (CHIKV). Gel profile comparisons showed that CHIKV at 3 DPI modulated the level of 13 proteins, and at 5 DPI 20 proteins. The amount of 10 putatively secreted proteins was regulated at both time points. These proteins were implicated in blood-feeding or in immunity, but many have no known function. CHIKV also modulated the quantity of proteins involved in several metabolic pathways and in cell signalling.
  
  
  CONCLUSIONS
  Our study constitutes the first analysis of the protein response of Aedes aegypti salivary glands infected with CHIKV. We found that the differentially regulated proteins in response to viral infection include structural proteins and enzymes for several metabolic pathways. Some may favour virus survival, replication and transmission, suggesting a subversion of the insect cell metabolism by arboviruses. For example, proteins involved in blood-feeding such as the short D7, an adenosine deaminase and inosine-uridine preferring nucleoside hydrolase, may favour virus transmission by exerting an increased anti-inflammatory effect. This would allow the vector to bite without the bite being detected. Other proteins, like the anti-freeze protein, may support vector protection.
authors.affiliation: Unité de Génétique Moléculaire des Bunyavirus, Paris, France.
authors.forename: Stephane
authors.initials: S
authors.lastname: Tchankouo-Nguetcheu
authors.forename: Edouard
authors.initials: E
authors.lastname: Bourguet
authors.forename: Pascal
authors.initials: P
authors.lastname: Lenormand
authors.forename: Jean-Claude
authors.initials: JC
authors.lastname: Rousselle
authors.forename: Abdelkader
authors.initials: A
authors.lastname: Namane
authors.forename: Valerie
authors.initials: V
authors.lastname: Choumet
mesh_terms: D000330:Aedes / Q000378:metabolism / Q000502:physiology / Q000821:virology*; D018354:Alphavirus Infections / Q000635:transmission* / Q000821:virology; D000818:Animals; D065632:Chikungunya Fever; D002646:Chikungunya virus / Q000502:physiology*; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D054884:Host-Pathogen Interactions; D006801:Humans; D019476:Insect Proteins / Q000302:isolation & purification / Q000378:metabolism*; D007303:Insect Vectors / Q000378:metabolism / Q000502:physiology / Q000821:virology*; D013058:Mass Spectrometry; D040901:Proteomics; D012367:RNA, Viral / Q000032:analysis / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012469:Salivary Glands / Q000821:virology
chemical_list: D019476:Insect Proteins; D012367:RNA, Viral