Pollen record during the Eemian from the Fuentillejo maar-lake sequence (Ciudad Real, Spain)

The Fuentillejo maar is located in the Central Spanish Volcanic Field of Campo de Calatrava (Ciudad Real). Fuentillejo maar-Iake is a c10sed system covering over 142 m depth oflacustrine sediments; it is one ofthe best examples oflong and continuous cores at terrestrial site from the Iberian Peninsula. PalynoIogical, mineralogical and sedimentary facies analysis were performed to characterize the sedimentary record during the Last Interglacial. In core FUENT-l this period (dated in 133 ka-120 ka) is detected between 45,90-56,90 m depth. Sedimentology point of view is characterized by develop of lacustrine facies, fineIy laminated black-brown doIomicrite mud and sapropeIIayers (Sedimentary Units 16,6-17-18). The vegetation is characterised by high polIen taxa diversity (around 50 polIen taxa of terrestriaI types, 5 polIen taxa of aquatic types, spores and 9 types of non palynological microfossils-NPM) together with a high content in the Mediterranean and mesic forest components (Quercus evergreen, Oleaceae, Quercus decidous and CoryIus), tipical ofwarm and humid conditions, and a few content on Artemisia, Pinus and Juniperus taxa (typicaI of coId or warm arid phases). The scarce forest development can be interpreted from the polIen record of mesophilus and thermophilous vegetation of the FUENT-1 sequence, in which only 40-50% of total polIen come from arboreaI associations. These vaIues for arboreal pollen content are low compared with other European polIen sequences.

A Recombinant Sal k 1 Isoform as an Alternative to the Polymorphic Allergen from Salsola kali Pollen for Allergy Diagnosis

The incidence of Amaranthaceae pollen allergy has increased due to the desertification occurring in many countries. In some regions of Spain, Salsola kali is the main cause of pollinosis, at almost the same level as olive and grass pollen. Sal k 1 - the sensitization marker of S. kali pollinosis - is used in clinical diagnosis, but is purified at a low yield from pollen. We aimed to produce a recombinant (r)Sal k 1 able to span the structural and immunological properties of the natural isoforms from pollen, and validate its potential use for diagnosis. METHODS: Specific cDNA was amplified by PCR, cloned into the pET41b vector and used to transform BL21 (DE3) Escherichia coli cells. Immunoblotting, ELISA, basophil activation and skin-prick tests were used to validate the recombinant protein against Sal k 1 isolated from pollen. Sera and blood cells from S. kali pollen-sensitized patients and specific monoclonal and polyclonal antisera were used. RESULTS: rSal k 1 was produced in bacteria with a yield of 7.5 mg/l of cell culture. The protein was purified to homogeneity and structural and immunologically validated against the natural form. rSal k 1 exhibited a higher IgE cross-reactivity with plant-derived food extracts such as peanut, almond or tomato than with pollen sources such as Platanus acerifolia and Oleaceae members. CONCLUSIONS: rSal k 1 expressed in bacteria retains intact structural and immunological properties in comparison to the pollen-derived allergen. It spans the immunological properties of most of the isoforms found in pollen, and it might substitute natural Sal k 1 in clinical diagnosis.