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Species of Hydrosmecta C. G. Thomson, occurring in eastern Canada, are studied and reviewed. Six species are recognized, and two of them are described as new to science. The new species are: Hydrosmecta canadensis Webster and Klimaszewski, new species, and Hydrosmecta minutissimoides Webster and Klimaszewski, new species. Two species described in the USA are recorded from Canada and New Brunswick for the first time: Hydrosmecta caduca Casey and Hydrosmecta dulcis Casey. New distribution and collection data, diagnoses, a key for species identification, and images of habitus and genital structures are provided. Hydrosmecta newfoundlandica Klimaszewski and Langor, 2011, is transferred to the genus Atheta Thomson based on morphology of genital structures.
Forty new provincial records, including two new aleocharine species for the province of Manitoba (Coleoptera: Staphylinidae) are provided. The two new species, Acrotona manitobensis Klimaszewski and Godin, new species, and Atheta manitobae Klimaszewski and Godin, new species, are described and illustrated. Habitat information and new locality records are provided for the newly recorded species. The current number of Aleocharinae in Manitoba stands at 120 species, including 40 new records and two new species described here. A checklist of all currently recorded species from the province, with their distribution records in Canada and USA, is included.
A new subgenus, Hydrosmectomorpha Klimaszewski and Webster, of the genus Atheta C. G. Thomson (Coleoptera: Staphylinidae: Aleocharinae) is erected to accommodate three new species and Atheta newfoundlandica (Klimaszewski and Langor). The new species are: Atheta (Hydrosmectomorpha) meduxnekeagensis Webster and Klimaszewski, new species; Atheta (Hydrosmectomorpha) quebecensis Webster and Klimaszewski, new species, Atheta (Hydrosmectomorpha) vincenti Webster and Klimaszewski, new species. The new species are described, illustrated, and a key is provided. Atheta newfoundlandica (Klimaszewski and Langor), was recently transferred from Hydrosmecta C.G. Thomson to an unspecified subgenus of Atheta. New habitat/collection data are presented for the treated species.
Non-standard errors
(2021)
In statistics, samples are drawn from a population in a data-generating process (DGP). Standard errors measure the uncertainty in sample estimates of population parameters. In science, evidence is generated to test hypotheses in an evidence-generating process (EGP). We claim that EGP variation across researchers adds uncertainty: non-standard errors. To study them, we let 164 teams test six hypotheses on the same sample. We find that non-standard errors are sizeable, on par with standard errors. Their size (i) co-varies only weakly with team merits, reproducibility, or peer rating, (ii) declines significantly after peer-feedback, and (iii) is underestimated by participants.
Of the 16 non-structural proteins (Nsps) encoded by SARS CoV-2, Nsp3 is the largest and plays important roles in the viral life cycle. Being a large, multidomain, transmembrane protein, Nsp3 has been the most challenging Nsp to characterize. Encoded within Nsp3 is the papain-like protease PLpro domain that cleaves not only the viral protein but also polyubiquitin and the ubiquitin-like modifier ISG15 from host cells. We here compare the interactors of PLpro and Nsp3 and find a largely overlapping interactome. Intriguingly, we find that near full length Nsp3 is a more active protease compared to the minimal catalytic domain of PLpro. Using a MALDI-TOF based assay, we screen 1971 approved clinical compounds and identify five compounds that inhibit PLpro with IC50s in the low micromolar range but showed cross reactivity with other human deubiquitinases and had no significant antiviral activity in cellular SARS-CoV-2 infection assays. We therefore looked for alternative methods to block PLpro activity and engineered competitive nanobodies that bind to PLpro at the substrate binding site with nanomolar affinity thus inhibiting the enzyme. Our work highlights the importance of studying Nsp3 and provides tools and valuable insights to investigate Nsp3 biology during the viral infection cycle.
Of the 16 non-structural proteins (Nsps) encoded by SARS CoV-2, Nsp3 is the largest and plays important roles in the viral life cycle. Being a large, multidomain, transmembrane protein, Nsp3 has been the most challenging Nsp to characterize. Encoded within Nsp3 is the papain-like protease domain (PLpro) that cleaves not only the viral polypeptide but also K48-linked polyubiquitin and the ubiquitin-like modifier, ISG15, from host cell proteins. We here compare the interactors of PLpro and Nsp3 and find a largely overlapping interactome. Intriguingly, we find that near full length Nsp3 is a more active protease compared to the minimal catalytic domain of PLpro. Using a MALDI-TOF based assay, we screen 1971 approved clinical compounds and identify five compounds that inhibit PLpro with IC50s in the low micromolar range but showed cross reactivity with other human deubiquitinases and had no significant antiviral activity in cellular SARS-CoV-2 infection assays. We therefore looked for alternative methods to block PLpro activity and engineered competitive nanobodies that bind to PLpro at the substrate binding site with nanomolar affinity thus inhibiting the enzyme. Our work highlights the importance of studying Nsp3 and provides tools and valuable insights to investigate Nsp3 biology during the viral infection cycle.