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Celikgil, A.

Publications and source records attributed to Celikgil, A..

3 recordsLinked to original sources

Urbanisation drives biodiversity loss, fitness decline and community shifts in cavity-nesting Hymenoptera

Urbanisation is reshaping landscapes worldwide, posing challenges to biodiversity and ecosystem function. Cavity-nesting Hymenoptera, including bees and wasps, deliver vital ecological services but are increasingly vulnerable to urbanisation. In this citizen science-based study, we deployed 286 trap nests across Leipzig and Hamburg (Germany) to investigate how urbanisation and landscape-scale environmental features influence the diversity, community composition, reproductive success, offspring survival and demographic status of these insects. Using Bayesian hierarchical and phylogenetically informed modelling, we found that urbanisation significantly reduced species richness, reproductive output and offspring survival in both guilds, despite stable nesting activity, suggesting potential ecological trap effects. For bees, urbanisation also reduced the probability of nests functioning as demographic sources. Environmental drivers shaped responses in taxon-specific ways: bee richness and survival increased with landscape diversity but declined with fragmentation, while wasp richness and nesting declined with higher temperatures, though survival increased with more green cover. Bee nests were more likely to serve as demographic sources in higher temperatures. Community composition responses also diverged; bee communities shifted via increased species turnover, while wasp assemblages remained relatively stable. Temperature was a major driver of compositional dissimilarity in both groups, whereas landscape diversity was associated with homogenisation in bees and diversification in wasps. Our findings demonstrate that cities filter cavity-nesting Hymenoptera through multiple ecological pathways, highlighting the need for differentiated conservation strategies that consider both habitat structure and taxon-specific responses.

ecology↗

SARS-CoV-2 multi-antigen protein microarray for detailed characterization of antibody responses in COVID-19 patients

Antibodies against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) target multiple epitopes on different domains of the spike protein, and other SARS-CoV-2 proteins. We developed a SARS-CoV-2 multi-antigen protein microarray with the nucleocapsid, spike and its domains (S1, S2), and variants with single (D614G, E484K, N501Y) or double substitutions (N501Y/Deletion69/70), allowing a more detailed high-throughput analysis of the antibody repertoire following infection. The assay was demonstrated to be reliable and comparable to ELISA. We analyzed antibodies from 18 COVID-19 patients and 12 recovered convalescent donors. S IgG level was higher than N IgG in most of the COVID-19 patients, receptor-binding domain of S1 showed high reactivity, but no antibodies were detected against heptad repeat domain 2 of S2. Furthermore, antibodies were detected against S variants with single and double substitutions in COVID-19 patients who were infected with SARS-CoV-2 early in the pandemic. Here we demonstrated that SARS-CoV-2 multi-antigen protein microarray is a powerful tool for detailed characterization of antibody responses, with potential utility in understanding the disease progress and assessing current vaccines and therapies against evolving SARS-CoV-2.

biochemistry↗

Characterization of the SARS-CoV-2 S Protein: Biophysical, Biochemical, Structural, and Antigenic Analysis

Coronavirus disease 2019 (COVID-19) is a global health crisis caused by the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and there is a critical need to produce large quantities of high-quality SARS-CoV-2 Spike (S) protein for use in both clinical and basic science settings. To address this need, we have evaluated the expression and purification of two previously reported S protein constructs in Expi293F and ExpiCHO-S cells, two different cell lines selected for increased expression of secreted glycoproteins. We show that ExpiCHO-S cells produce enhanced yields of both SARS-CoV-2 S proteins. Biochemical, biophysical, and structural (cryo-EM) characterization of the SARS-CoV-2 S proteins produced in both cell lines demonstrate that the reported purification strategy yields high quality S protein (non-aggregated, uniform material with appropriate biochemical and biophysical properties). Importantly, we show that multiple preparations of these two recombinant S proteins from either cell line exhibit identical behavior in two different serology assays. We also evaluate the specificity of S protein-mediated host cell binding by examining interactions with proposed binding partners in the human secretome. In addition, the antigenicity of these proteins is demonstrated by standard ELISAs, and in a flexible protein microarray format. Collectively, we establish an array of metrics for ensuring the production of high-quality S protein to support clinical, biological, biochemical, structural and mechanistic studies to combat the global pandemic caused by SARS-CoV-2.

biochemistry↗