Authors’ contributions SL executed the Leptspiral isolation, MAT, PCR and MLST experiments, analyzed the data and drafted the manuscript; CZ participated in the analysis of MLST results; DW participated in the study design; XW participated the MLST experiments; KT participated in the rodents Trapping; XL and XJ provided the reference strains of L. interrogans; YN provided the rabbit anti-Leptospira serum; YL contributed to the culture of leptospiral strains and the MAT

experiments; GY and JZ participated in rodents trapping and Leptospira isolation. GT participated in the study design; JY critically revised the manuscript; all authors read and approved the final manuscript.”
“Background Periodontal CP673451 supplier disease is a bacterially induced and highly common chronic inflammatory condition OICR-9429 in humans, and severe periodontal disease (periodontitis)

remains the major cause of tooth loss in adult population worldwide [1]. Dysregulated host response to pathogenic plaque biofilm critically contributes to destructive inflammation resulting in tissue damage and alveolar bone loss [2]. Porphyromonas gingivalis is a keystone periodontal pathogen in the mixed microbial community and it releases copious amount of lipopolysaccharide (LPS) which perpetually interacts with host cells, thereby significantly contributing to periodontal pathogenesis [1–4]. LPS is a potent immuno-inflammatory modulator which causes serious complications in host. It is comprised of three major components viz. outermost O-antigen, core oligosaccharide regions and innermost lipid A [3]. Lipid A is the biologically most active component of LPS that imparts the endotoxin activity. Its structure differs widely among Gram-negative bacteria species depending on the differences in composition of attached

fatty acids, number of phosphorylation sites and substituted groups attached to the phosphate residues [3]. The canonical lipid A structure in Escherichia coli LPS is a hexa-acylated diphosphorylated glucosamine disaccharide. Previous studies have shown that P. gingivalis possesses highly heterogeneous lipid A structures containing penta-acylated LPS1690 and tetra-acylated LPS1435/1449, and this structural discrepancy may critically account for contrasting biological activities induced by P. gingivalis LPS [3, 4]. Human gingival fibroblasts (HGFs) are the major cell type Atezolizumab in human gingiva [5–7]. They play a key role in maintenance and remodeling of extra cellular matrix (ECM) by producing various structural components, such as collagen, elastin, glycoprotein and glycosaminoglycans. In addition, HGFs also synthesize and secrete various members of matrix metalloproteinases (MMPs) in response to P. gingivalis LPS challenge, which ultimately contribute to periodontal tissue destruction [8]. MMPs are a family of structurally and functionally related proteolytic enzymes containing a zinc-binding catalytic domain and they are active against the components of ECM [8–10].