Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei

Markus Linder, Geza Szilvay, Tiina Nakari-Setälä, Hans Söderlund, Merja Penttilä

Research output: Contribution to journalArticleScientificpeer-review

100 Citations (Scopus)

Abstract

Hydrophobins are surface-active proteins produced by filamentous fungi, where they seem to be ubiquitous. They have a variety of roles in fungal physiology related to surface phenomena, such as adhesion, formation of surface layers, and lowering of surface tension. Hydrophobins can be divided into two classes based on the hydropathy profile of their primary sequence. We have studied the adhesion behavior of two Trichoderma reesei class II hydrophobins, HFBI and HFBII, as isolated proteins and as fusion proteins. Both hydrophobins were produced as C-terminal fusions to the core of the hydrolytic enzyme endoglucanase I from the same organism. It was shown that as a fusion partner, HFBI causes the fusion protein to efficiently immobilize to hydrophobic surfaces, such as silanized glass and Teflon. The properties of the surface-bound protein were analyzed by the enzymatic activity of the endoglucanase domain, by surface plasmon resonance (Biacore), and by a quartz crystal microbalance. We found that the HFBI fusion forms a tightly bound, rigid surface layer on a hydrophobic support. The HFBI domain also causes the fusion protein to polymerize in solution, possibly to a decamer. Although isolated HFBII binds efficiently to surfaces, it does not cause immobilization as a fusion partner, nor does it cause polymerization of the fusion protein in solution. The findings give new information on how hydrophobins function and how they can be used to immobilize fusion proteins
Original languageEnglish
Pages (from-to)2257-2266
JournalProtein Science
Volume11
Issue number9
DOIs
Publication statusPublished - 2002
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Fusion reactions
Adhesion
Proteins
Membrane Proteins
Quartz Crystal Microbalance Techniques
Cellulases
Surface Tension
Surface Plasmon Resonance
Cellulase
Polytetrafluoroethylene
Polymerization
Immobilization
Surface phenomena
Glass
1-(heptafluorobutyryl)imidazole
Fungi
Quartz crystal microbalances
Physiology
Surface plasmon resonance

Keywords

  • protein adhesion
  • hydrophobins
  • supramolecular assembly
  • Trichoderma reesei

Cite this

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title = "Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei",
abstract = "Hydrophobins are surface-active proteins produced by filamentous fungi, where they seem to be ubiquitous. They have a variety of roles in fungal physiology related to surface phenomena, such as adhesion, formation of surface layers, and lowering of surface tension. Hydrophobins can be divided into two classes based on the hydropathy profile of their primary sequence. We have studied the adhesion behavior of two Trichoderma reesei class II hydrophobins, HFBI and HFBII, as isolated proteins and as fusion proteins. Both hydrophobins were produced as C-terminal fusions to the core of the hydrolytic enzyme endoglucanase I from the same organism. It was shown that as a fusion partner, HFBI causes the fusion protein to efficiently immobilize to hydrophobic surfaces, such as silanized glass and Teflon. The properties of the surface-bound protein were analyzed by the enzymatic activity of the endoglucanase domain, by surface plasmon resonance (Biacore), and by a quartz crystal microbalance. We found that the HFBI fusion forms a tightly bound, rigid surface layer on a hydrophobic support. The HFBI domain also causes the fusion protein to polymerize in solution, possibly to a decamer. Although isolated HFBII binds efficiently to surfaces, it does not cause immobilization as a fusion partner, nor does it cause polymerization of the fusion protein in solution. The findings give new information on how hydrophobins function and how they can be used to immobilize fusion proteins",
keywords = "protein adhesion, hydrophobins, supramolecular assembly, Trichoderma reesei",
author = "Markus Linder and Geza Szilvay and Tiina Nakari-Set{\"a}l{\"a} and Hans S{\"o}derlund and Merja Penttil{\"a}",
year = "2002",
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Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei. / Linder, Markus; Szilvay, Geza; Nakari-Setälä, Tiina; Söderlund, Hans; Penttilä, Merja.

In: Protein Science, Vol. 11, No. 9, 2002, p. 2257-2266.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei

AU - Linder, Markus

AU - Szilvay, Geza

AU - Nakari-Setälä, Tiina

AU - Söderlund, Hans

AU - Penttilä, Merja

PY - 2002

Y1 - 2002

N2 - Hydrophobins are surface-active proteins produced by filamentous fungi, where they seem to be ubiquitous. They have a variety of roles in fungal physiology related to surface phenomena, such as adhesion, formation of surface layers, and lowering of surface tension. Hydrophobins can be divided into two classes based on the hydropathy profile of their primary sequence. We have studied the adhesion behavior of two Trichoderma reesei class II hydrophobins, HFBI and HFBII, as isolated proteins and as fusion proteins. Both hydrophobins were produced as C-terminal fusions to the core of the hydrolytic enzyme endoglucanase I from the same organism. It was shown that as a fusion partner, HFBI causes the fusion protein to efficiently immobilize to hydrophobic surfaces, such as silanized glass and Teflon. The properties of the surface-bound protein were analyzed by the enzymatic activity of the endoglucanase domain, by surface plasmon resonance (Biacore), and by a quartz crystal microbalance. We found that the HFBI fusion forms a tightly bound, rigid surface layer on a hydrophobic support. The HFBI domain also causes the fusion protein to polymerize in solution, possibly to a decamer. Although isolated HFBII binds efficiently to surfaces, it does not cause immobilization as a fusion partner, nor does it cause polymerization of the fusion protein in solution. The findings give new information on how hydrophobins function and how they can be used to immobilize fusion proteins

AB - Hydrophobins are surface-active proteins produced by filamentous fungi, where they seem to be ubiquitous. They have a variety of roles in fungal physiology related to surface phenomena, such as adhesion, formation of surface layers, and lowering of surface tension. Hydrophobins can be divided into two classes based on the hydropathy profile of their primary sequence. We have studied the adhesion behavior of two Trichoderma reesei class II hydrophobins, HFBI and HFBII, as isolated proteins and as fusion proteins. Both hydrophobins were produced as C-terminal fusions to the core of the hydrolytic enzyme endoglucanase I from the same organism. It was shown that as a fusion partner, HFBI causes the fusion protein to efficiently immobilize to hydrophobic surfaces, such as silanized glass and Teflon. The properties of the surface-bound protein were analyzed by the enzymatic activity of the endoglucanase domain, by surface plasmon resonance (Biacore), and by a quartz crystal microbalance. We found that the HFBI fusion forms a tightly bound, rigid surface layer on a hydrophobic support. The HFBI domain also causes the fusion protein to polymerize in solution, possibly to a decamer. Although isolated HFBII binds efficiently to surfaces, it does not cause immobilization as a fusion partner, nor does it cause polymerization of the fusion protein in solution. The findings give new information on how hydrophobins function and how they can be used to immobilize fusion proteins

KW - protein adhesion

KW - hydrophobins

KW - supramolecular assembly

KW - Trichoderma reesei

U2 - https://doi.org/10.1110/ps.0207902

DO - https://doi.org/10.1110/ps.0207902

M3 - Article

VL - 11

SP - 2257

EP - 2266

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 9

ER -