Publications by authors named "C Hanus"

Archaea produce various protein filaments with specialised functions. While some archaea produce only one type of filament, the archaeal model species Sulfolobus acidocaldarius generates four. These include rotary swimming propellers analogous to bacterial flagella (archaella), pili for twitching motility (Aap), adhesive fibres (threads), and filaments facilitating homologous recombination upon UV stress (UV pili).

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Amongst the major types of archaeal filaments, several have been shown to closely resemble bacterial homologues of the Type IV pili (T4P). Within Sulfolobales, member species encode for three types of T4P, namely the archaellum, the UV-inducible pilus system (Ups) and the archaeal adhesive pilus (Aap). Whereas the archaellum functions primarily in swimming motility, and the Ups in UV-induced cell aggregation and DNA-exchange, the Aap plays an important role in adhesion and twitching motility.

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Most membrane proteins are modified by covalent addition of complex sugars through N- and O-glycosylation. Unlike proteins, glycans do not typically adopt specific secondary structures and remain very mobile, shielding potentially large fractions of protein surface. High glycan conformational freedom hinders complete structural elucidation of glycoproteins.

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Surface layers (S-layers) are resilient two-dimensional protein lattices that encapsulate many bacteria and most archaea. In archaea, S-layers usually form the only structural component of the cell wall and thus act as the final frontier between the cell and its environment. Therefore, S-layers are crucial for supporting microbial life.

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Article Synopsis
  • N-glycosylation is a critical posttranslational modification that affects protein properties like activity and solubility, particularly for glycosyltransferases such as human Gb3/CD77 synthase, which is essential for synthesizing important glycotopes that serve as receptors for pathogens.
  • The study reveals that N-glycosylation at specific sites is necessary for the enzymatic activity of Gb3/CD77 synthase, with both N-glycans being crucial for enzyme secretion and activity, while individual glycans lead to reduced function.
  • In silico modeling indicates that one of the N-glycans is strategically positioned near the enzyme's active site, suggesting it may influence enzymatic activity through allosteric mechanisms
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