Fructobacillus cardui sp. nov., isolated from a thistle (Carduus nutans) flower.

A Fructobacillus strain was isolated from the flower of a nodding thistle (Carduus nutans) collected in Bavaria, Germany. The strain is Gram-positive, rod-shaped, non-motile, non-sporulating, catalase- and oxidase-negative, and facultatively anaerobic. Growth can be detected at 10-37 °C and pH 4 to 9. The genome size is about 1.56 Mbp and the G+C content is 43.76 mol%. Assignment to the genus Fructobacillus was done by average nucleotide identity (ANI), 16S rRNA gene sequence and multilocus sequence analyses. Calculations of ANI and digital DNA-DNA hybridization values indicate a novel species with Fructobacillus tropaeoli DSM 23246T (93.58% ANI and 57.9 % dDDH) being its closest relative. Therefore, a new species named Fructobacillus cardui sp. nov. with TMW 2.2452T (=DSM 113480T=CECT 30515T) as type strain is proposed.

Optimization of a cultivation procedure to selectively isolate lactic acid bacteria from insects.

AIMS: Natural niches and transmission routes of lactic acid bacteria (LAB) are highly versatile. Proposed routes of transmission to food fermentations are from plant material via insects or vice versa. This study aimed to establish a method for the selective isolation of LAB from insects. METHODS AND RESULTS: Varied parameters that influence growth and selectivity are temperature, type of carbohydrate and atmosphere. Additionally, the effects of antibiotics to suppress non-LAB species were evaluated. A model consortium consisting of 12 species representing different lifestyles was inoculated in a growth medium to identify conditions for the highest diversity and recovery rate. The method was applied to isolate LAB from Drosophila melanogaster, Sitotroga cerealella, Tribolium castaneum and Tenebrio molitor. Isolated species were Leuconostoc mesenteroides, Paucilactobacillus vaccinostercus and Lactiplantibacillus plantarum from D. melanogaster and L. mesenteroides, Pediococcus pentosaceus and Latilactobacillus curvatus from T. molitor. No LAB could be isolated from T. castaneum and S. cerealella. 16S rDNA amplicon sequencing of DNA obtained from insects corroborated part of our results. CONCLUSION: A combination of different enrichment conditions ensures a high probability to isolate LAB species from insects and can be helpful above already known non-cultivation methods. SIGNIFICANCE AND IMPACT OF THE STUDY: The novel method allows to selectively isolate LAB from insects and the strategy of the method is of interest to study other niches.

Correction to: Cerebrospinal fluid amyloid-ß 2-42 is decreased in Alzheimer's, but not in frontotemporal dementia.

The respective first and last authors of this article, Mirko Bibl and Jens Wiltfang, would like to clarify the issue of the seeming duplicate publication of a figure in two articles.

Characterization of cerebrospinal fluid aminoterminally truncated and oxidized amyloid-ß peptides.

PURPOSE: Carboxyterminally elongated and aminoterminally truncated Aß peptides as well as their pyroglutamate and oxidized derivates are major constituents of human amyloid plaques. The objective of the present study was to characterize aminoterminally truncated or oxidized Aß38, Aß40, and Aß42 peptide species in immunoprecipitated human cerebrospinal fluid (CSF). EXPERIMENTAL DESIGN: We invented a novel sequential aminoterminally and carboxyterminally specific immunoprecipitation protocol and used the Aß-SDS-PAGE/immunoblot for subsequent analysis of CSF Aß peptide patterns. RESULTS: In the present study, we identified the aminoterminally truncated Aß peptides 2-40 and 2-42 as well as oxidized forms of Aß1-38 and Aß1-42 in CSF. Our protocol allowed the quantification of a pattern of Aß peptides 1-38(ox), 2-40, and 2-42 in addition to the well known panel of Aß 1-37, 1-38, 1-39, 1-40, 1-40(ox), and 1-42 in a group of seven patients with peripheral polyneuropathy. CONCLUSIONS AND CLINICAL RELEVANCE: In the present approach, we could broaden the range of quantifiable Aß peptides described in previous studies (i.e., 1-37, 1-38, 1-39, 1-40, 1-40(ox), and 1-42) by Aß 1-38(ox), 2-40, and 2-42. An exact analysis of CSF Aß peptides regarding their carboxy- and aminoterminus as well as posttranslational modification seems promising with respect to diagnostic and pathogenic aspects.

Cerebrospinal fluid amyloid-ß 2-42 is decreased in Alzheimer's, but not in frontotemporal dementia.

Alzheimer's dementia (AD) and frontotemporal dementias (FTD) are common and their clinical differential diagnosis may be complicated by overlapping symptoms, which is why biomarkers may have an important role to play. Cerebrospinal fluids (CSF) Aß2-42 and 1-42 have been shown to be similarly decreased in AD, but 1-42 did not display sufficient specificity for exclusion of other dementias from AD. The objective of the present study was to clarify the diagnostic value of Aß2-42 peptides for the differential diagnosis of AD from FTD. For this purpose, 20 non-demented disease controls (NDC), 22 patients with AD and 17 with FTD were comparatively analysed by a novel sequential aminoterminally and carboxyterminally specific immunoprecipitation protocol with subsequent Aß-SDS-PAGE/immunoblot, allowing the quantification of peptides 1-38(ox), 2-40 and 2-42 along with Aß 1-37, 1-38, 1-39, 1-40, 1-40(ox) and 1-42. CSF Aß1-42 was decreased in AD as compared to NDC, but not to FTD. In a subgroup of the patients analyzed, the decrease of Abeta2-42 in AD was evident as compared to both NDC and FTD. Aß1-38 was decreased in FTD as compared to NDC and AD. For differentiating AD from FTD, Aß1-42 demonstrated sufficient diagnostic accuracies only when combined with Aß1-38. Aß2-42 yielded diagnostic accuracies of over 85 % as a single marker. These accuracy figures could be improved by combining Aß2-42 to Aß1-38. Aß2-42 seems to be a promising biomarker for differentiating AD from other degenerative dementias, such as FTD.

Aminoterminally truncated and oxidized amyloid-ß peptides in the cerebrospinal fluid of Alzheimer's disease patients.

Carboxyterminally elongated and aminoterminally truncated amyloid-ß (Aß) peptides and their oxidized derivates are major constituents of human amyloid plaques. The objective of the present study was to clarify the diagnostic impact of the Aß peptides 1-38ox, 2-40, and 2-42 peptides on the neurochemical cerebrospinal fluid (CSF) diagnosis of Alzheimer's disease (AD). For this purpose, 22 patients with AD and 20 non-demented disease controls (NDC) were comparatively analyzed for their cerebrospinal fluid pattern of Aß1-38ox, Aß2-40, and Aß2-42 along with Aß1-37, Aß1-38, Aß1-39, Aß1-40, Aß1-40ox, and Aß1-42 using a novel sequential aminoterminally and carboxyterminally specific immunoprecipitation protocol and subsequent analysis in the Aß-SDS-PAGE/immunoblot. The Aß peptides 1-38ox, 2-40, and 2-42 could not be consistently detected in the investigated CSF samples, which applied to samples from AD and NDC patients alike. Otherwise, our approach revealed a striking decrease of Aß1-42 and Aß2-42, but not of Aß1-38ox and Aß2-40 in AD. Both Aß1-42 and Aß2-42 reached reasonable accuracies for diagnosing AD alone as well as in relation to Aß1-40, Aß1-38, or the sum of all measured Aß peptides. Aß1-38ox was negatively correlated to the Mini-Mental Status Examination score of AD patients, indicating that this peptide to linked to disease severity. We conclude that an exact analysis of CSF Aß peptides regarding their carboxy- and aminoterminus as well as posttranslational modification may be a promising approach for diagnosing and tracking AD.