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Characterization of nit sheath protein functions and transglutaminase-mediated cross-linking in the human head louse, Pediculus humanus capitis

DC Field Value Language
dc.contributor.authorKim, Ju Hyeon-
dc.contributor.authorLee, Do Eun-
dc.contributor.authorPark, SangYoun-
dc.contributor.authorClark, John M.-
dc.contributor.authorLee, Si Hyeock-
dc.date.accessioned2021-09-02T04:59:17Z-
dc.date.available2021-09-02T14:00:19Z-
dc.date.issued2021-08-24-
dc.identifier.citationParasites & Vectors. 2021 Aug 24;14(1):425ko_KR
dc.identifier.issn1756-3305-
dc.identifier.urihttps://hdl.handle.net/10371/174860-
dc.description.abstractBackground
Head louse females secrete liquid glue during oviposition, which is solidified to form the nit sheath over the egg. Recently, two homologous proteins, named louse nit sheath protein (LNSP) 1 and LNSP 2, were identified as adhesive proteins but the precise mechanism of nit sheath solidification is unknown.

Methods
We determined the temporal transcriptome profiles of the head louse accessory glands plus oviduct, from which putative major structural proteins and those with functional importance were deduced. A series of RNA interference (RNAi) experiments and treatment of an inhibitor were conducted to elucidate the function and action mechanism of each component.

Results
By transcriptome profiling of genes expressed in the louse accessory glands plus uterus, the LNSP1 and LNSP2 along with two hypothetical proteins were confirmed to be the major structural proteins. In addition, several proteins with functional importance, including transglutaminase (TG), defensin 1 and defensin 2, were identified. When LNSP1 was knocked down via RNA interference, most eggs became nonviable via desiccation, suggesting its role in desiccation resistance. Knockdown of LNSP2, however, resulted in oviposition failure, which suggests that LNSP2 may serve as the basic platform to form the nit sheath and may have an additional function of lubrication. Knockdown of TG also impaired egg hatching, demonstrating its role in the cross-linking of nit sheath proteins. The role of TG in cross-linking was further confirmed by injecting or hair coating of GGsTop, a TG inhibitor.

Conclusions
Both LNSP1 and LNSP2 are essential for maintaining egg viability besides their function as glue. The TG-mediated cross-linking plays critical roles in water preservation that are essential for ensuring normal embryogenesis. TG-mediated cross-linking mechanism can be employed as a therapeutic target to control human louse eggs, and any topically applied TG inhibitors can be exploited as potential ovicidal agents.

Graphical abstract
ko_KR
dc.description.sponsorshipThis work was supported by a grant from the National Institutes of Health/National Institute for Allergy and Infectious Disease (5R01AI045062-06) to JM Clark and SH Lee. DE Lee was supported in part by the Brain Korea 21 Plus program.ko_KR
dc.language.isoenko_KR
dc.publisherBMCko_KR
dc.subjectHead louse-
dc.subjectNit sheath-
dc.subjectLNSP-
dc.subjectTransglutaminase-
dc.subjectCross-linking-
dc.titleCharacterization of nit sheath protein functions and transglutaminase-mediated cross-linking in the human head louse, Pediculus humanus capitisko_KR
dc.typeArticleko_KR
dc.contributor.AlternativeAuthor김주현-
dc.contributor.AlternativeAuthor이도은-
dc.contributor.AlternativeAuthor박상윤-
dc.contributor.AlternativeAuthor이시혁-
dc.identifier.doi10.1186/s13071-021-04914-z-
dc.citation.journaltitleParasites & Vectorsko_KR
dc.language.rfc3066en-
dc.rights.holderThe Author(s)-
dc.date.updated2021-08-29T03:12:28Z-
dc.citation.number1ko_KR
dc.citation.startpage425ko_KR
dc.citation.volume14ko_KR
Appears in Collections:
College of Agriculture and Life Sciences (농업생명과학대학)Research Institute of Agriculture and Life Sciences (농업생명과학연구원)Journal Papers (저널논문_농업생명과학연구원)
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