Whole-Chain Tick Saliva Proteins Presented on Hepatitis B Virus Capsid-Like Particles Induce High-Titered Antibodies with Neutralizing Potential

scientific article published on 9 September 2015

Whole-Chain Tick Saliva Proteins Presented on Hepatitis B Virus Capsid-Like Particles Induce High-Titered Antibodies with Neutralizing Potential is …
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scholarly articleQ13442814

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P819ADS bibcode2015PLoSO..1036180K
P356DOI10.1371/JOURNAL.PONE.0136180
P932PMC publication ID4564143
P698PubMed publication ID26352137
P5875ResearchGate publication ID281644403

P50authorMichael NassalQ55979346
P2093author name stringReinhard Wallich
Philipp Kolb
P2860cites workSalp15, an ixodes scapularis salivary protein, inhibits CD4(+) T cell activation.Q52597722
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The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assemblyQ40066232
Internal core protein cleavage leaves the hepatitis B virus capsid intact and enhances its capacity for surface display of heterologous whole chain proteinsQ41973374
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The molecular and biological analysis of ixodid ticks histamine release factorsQ42674533
Soluble cysteine-rich tick saliva proteins Salp15 and Iric-1 from E. coliQ43118363
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Core particles of hepatitis B virus as carrier for foreign epitopesQ43921072
Priming Th1 immunity to viral core particles is facilitated by trace amounts of RNA bound to its arginine-rich domainQ43982528
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Structure, assembly, and antigenicity of hepatitis B virus capsid proteins.Q45424169
A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formulaQ45519794
Quaternary structure is critical for protein display on capsid-like particles (CLPs): efficient generation of hepatitis B virus CLPs presenting monomeric but not dimeric and tetrameric fluorescent proteins.Q45554919
Total chemical synthesis of a gene for hepatitis B virus core protein and its functional characterizationQ45839728
Borrelia recurrentis employs a novel multifunctional surface protein with anti-complement, anti-opsonic and invasive potential to escape innate immunityQ21143848
The tick salivary protein Salp15 inhibits the killing of serum-sensitive Borrelia burgdorferi sensu lato isolatesQ24646938
Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core proteinQ24673603
The crystal structure of the human hepatitis B virus capsidQ27618957
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Antibodies against a tick protein, Salp15, protect mice from the Lyme disease agentQ33745554
Tick histamine release factor is critical for Ixodes scapularis engorgement and transmission of the lyme disease agentQ33760842
Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativityQ33966563
Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetesQ34245905
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A VLP library of C-terminally truncated Hepatitis B core proteins: correlation of RNA encapsidation with a Th1/Th2 switch in the immune responses of mice.Q35006090
Preferential protection of Borrelia burgdorferi sensu stricto by a Salp15 homologue in Ixodes ricinus saliva.Q35049649
T cell-independent type I antibody response against B cell epitopes expressed repetitively on recombinant virus particlesQ36262265
Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: implications for morphogenesis and organization of encapsidated RNA.Q36568551
Cross-species surface display of functional spirochetal lipoproteins by recombinant Borrelia burgdorferiQ36576612
Borrelia burgdorferi and tick proteins supporting pathogen persistence in the vectorQ36588072
Development of hepatitis B virus capsids into a whole-chain protein antigen display platform: new particulate Lyme disease vaccinesQ36948876
Tick vaccines and the control of tick-borne pathogensQ36993703
Native display of complete foreign protein domains on the surface of hepatitis B virus capsids.Q37163704
Interaction of the hepatitis B core antigen and the innate immune systemQ37200526
Ticks and tick-borne pathogens at the cutaneous interface: host defenses, tick countermeasures, and a suitable environment for pathogen establishmentQ37322741
Virus-like particles for the prevention of human papillomavirus-associated malignanciesQ37328475
The Plasmodium falciparum translationally controlled tumor protein (TCTP) is incorporated more efficiently into B cells than its human homologueQ37490702
Production of recombinant proteins by microbes and higher organismsQ37509309
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue9
P407language of work or nameEnglishQ1860
P921main subjectHepatitis B virusQ6844
salivaQ155925
P304page(s)e0136180
P577publication date2015-09-09
P1433published inPLOS OneQ564954
P1476titleWhole-Chain Tick Saliva Proteins Presented on Hepatitis B Virus Capsid-Like Particles Induce High-Titered Antibodies with Neutralizing Potential
P478volume10

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cites work (P2860)
Q61443712Hepatitis B virus core protein phosphorylation: Identification of the SRPK1 target sites and impact of their occupancy on RNA binding and capsid structure
Q93052249Salp15, a Multifunctional Protein From Tick Saliva With Potential Pharmaceutical Effects

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