Such fibrils are long, evenly spaced, radiating and mask hydropho

Such fibrils are long, evenly spaced, radiating and mask hydrophobic proteins [33]. The biochemical composition of the cell wall of hyphae and yeast cells of C. albicans has been investigated extensively [34, 35]. The C. albicans cell wall consists of two main layers: an outer layer of mannoproteins and an inner one that is composed of skeletal polysaccharides, such as chitin and β-1,3-glucans which confer strength and shape [34–36]. Although the basic cell wall components selleck compound of C. albicans remain the same for hyphal and yeast cells, the amount and exposure of polysaccharides, as well as its surface proteome differ significantly [35–37]. For example, the amount of chitin

in the hyphal cell wall is 3–5 times more than in the yeast cell wall, which could be relevant for the interaction with the host’s immune system [38]. Expression of a number of hypha-specific cell wall proteins, like agglutinin-like

sequence 3 (Als3) protein, is up-regulated during the yeast-hyphae switch [37, 39, 40]. Als3 is specifically recognized by Streptococcus gordonii Selleckchem Ruxolitinib and allowed bacteria to adhere to the hyphae [41] and is also involved in adhesion of S. aureus to C. albicans hyphae [25]. Interestingly, Als3 protein was localized exclusively along complete hyphae and was not observed in the head region of hyphae nor in yeast cell walls [42]. This is in line with the current observation that there is no significant difference in adhesion forces between S. aureus and the relatively young tip region compared to older regions of the hypha. Staphylococcal

adhesion forces varied within the two C. albicans strains involved in this study. This effect can possibly be explained by the differential expression of cell wall associated proteins, e.g. proteins belonging to the Als family. These proteins are recognized as amyloid proteins and able to rearrange to form β-sheets, see more depending on environmental conditions and the strain of C. albicans involved [39, 40, 43]. Agglutinin-like sequence 3 (Als3p) is known to play a major role in the adherence process between C. albicans hyphae and S. aureus[25] and we speculate that differences in the density of Als3p along on hyphae between C. albicans SC5314 and MB1 SN-38 ic50 account for the different adhesion forces measured with S. aureus. This speculation is supported by the increases in adhesion forces observed after 60 s surface delay, that may correspond to unzipping and rearrangement of a β-sheet-rich amyloid fibres [44]. Conclusion The findings generated from this study quantified S. aureus – C. albicans interactions and demonstrated that the head region of the hyphae is different from other hyphal regions. Therewith this study combines microbiology and physical-chemistry to yield a better understanding of the fast developing field of interkingdom interactions. Acknowledgements This work was funded by the University Medical Center Groningen, Groningen, The Netherlands. References 1.

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