Hydrophobins from Aspergillus species cannot be clearly divided into two classes

Publication: Research - peer-reviewJournal article – Annual report year: 2010

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@article{44e2f74a64044d61ac3df07bb4445add,
title = "Hydrophobins from Aspergillus species cannot be clearly divided into two classes",
publisher = "BioMed Central Ltd.",
author = "Jensen, {Britt Guillaume} and Andersen, {Mikael Rørdam} and Pedersen, {Mona Højgaard} and Frisvad, {Jens Christian} and Ib Søndergaard",
year = "2010",
doi = "10.1186/1756-0500-3-344",
volume = "3",
pages = "344",
journal = "B M C Research Notes",
issn = "1756-0500",

}

RIS

TY - JOUR

T1 - Hydrophobins from Aspergillus species cannot be clearly divided into two classes

A1 - Jensen,Britt Guillaume

A1 - Andersen,Mikael Rørdam

A1 - Pedersen,Mona Højgaard

A1 - Frisvad,Jens Christian

A1 - Søndergaard,Ib

AU - Jensen,Britt Guillaume

AU - Andersen,Mikael Rørdam

AU - Pedersen,Mona Højgaard

AU - Frisvad,Jens Christian

AU - Søndergaard,Ib

PB - BioMed Central Ltd.

PY - 2010

Y1 - 2010

N2 - Background Hydrophobins are a family of small secreted proteins with a characteristic pattern of eight cysteine residues found exclusively in filamentous fungi. They have originally been divided into two classes based on their physical properties and hydropathy patterns, and are involved in the attachment of hyphae to hydrophobic structures, the formation of aerial structures and appear to be involved in pathogenicity. Findings Analysis of nine genome sequences from seven Aspergilli revealed fifty hydrophobins, where each species displayed between two to eight hydrophobins. Twenty of the identified hydrophobins have not previously been described from these species. Apart from the cysteines, very little amino acid sequence homology was observed. Twenty-three of the identified hydrophobins could be classified as class I hydrophobins based on their conserved cysteine spacing pattern and hydropathy pattern. However twenty-six of the identified hydrophobins were intermediate forms. Notably, a single hydrophobin, ATEG_04730, from Aspergillus terreus displayed class II cysteine spacing and had a class II hydropathy pattern. Conclusion Fifty hydrophobins were identified in Aspergillus, all containing the characteristic eight cysteine pattern. Aspergillus terreus exhibited both class I and class II hydrophobins. This is the first report of an Aspergillus species with the potential to express both class I and class II hydrophobins. Many of the identified hydrophobins could not directly be allocated to either class I or class II.

AB - Background Hydrophobins are a family of small secreted proteins with a characteristic pattern of eight cysteine residues found exclusively in filamentous fungi. They have originally been divided into two classes based on their physical properties and hydropathy patterns, and are involved in the attachment of hyphae to hydrophobic structures, the formation of aerial structures and appear to be involved in pathogenicity. Findings Analysis of nine genome sequences from seven Aspergilli revealed fifty hydrophobins, where each species displayed between two to eight hydrophobins. Twenty of the identified hydrophobins have not previously been described from these species. Apart from the cysteines, very little amino acid sequence homology was observed. Twenty-three of the identified hydrophobins could be classified as class I hydrophobins based on their conserved cysteine spacing pattern and hydropathy pattern. However twenty-six of the identified hydrophobins were intermediate forms. Notably, a single hydrophobin, ATEG_04730, from Aspergillus terreus displayed class II cysteine spacing and had a class II hydropathy pattern. Conclusion Fifty hydrophobins were identified in Aspergillus, all containing the characteristic eight cysteine pattern. Aspergillus terreus exhibited both class I and class II hydrophobins. This is the first report of an Aspergillus species with the potential to express both class I and class II hydrophobins. Many of the identified hydrophobins could not directly be allocated to either class I or class II.

U2 - 10.1186/1756-0500-3-344

DO - 10.1186/1756-0500-3-344

JO - B M C Research Notes

JF - B M C Research Notes

SN - 1756-0500

VL - 3

SP - 344

ER -