FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells.

FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Research Abstract Details 

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FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Abstract Text:

Minghua Xu,Mitsunori Yamada,Mei Li,Hongqi Liu,Shu G Chen,Yiping W Han,

Fusobacterium nucleatum is a Gram-negative anaerobe associated with various human infections, including periodontal diseases and preterm birth. A novel FadA adhesin was recently identified for host-cell binding. It consists of 129 amino acid residues, with an 18-amino acid signal peptide. Expression of FadA in Escherichia coli enhanced bacterial binding to host epithelial and endothelial cells. In both E. coli and F. nucleatum, FadA exists in two forms, the intact pre-FadA and the secreted mature FadA (mFadA), with pre-FadA anchored in the inner membrane and mFadA secreted outside the bacteria. Pre-FadA and mFadA formed high M(r) complexes. When each form was purified to a single species, mFadA was soluble at neutral pH, whereas pre-FadA was insoluble. Pre-FadA became soluble when mixed with mFadA or under acidic pH. When fluorescence-labeled mFadA alone was added to the epithelial cells, no binding was detected. However, when mixed with nonlabeled pre-FadA, binding and invasion of mFadA into epithelial cells was observed. FadA is a unique bacterial adhesin/invasin in that it utilizes its own two forms for both structural and functional purposes. The pre-FadA-mFadA complex is probably anchored in the inner membrane and protrudes through the outer membrane. Internalization of the pre-FadA-mFadA ensures invasion of the bacteria into the host cells.

FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Publishing Authors By Initials

M Xu,M Yamada,M Li,H Liu,SG Chen,YW Han,

For similar animals: chordata: vertebrates: mammals: lagomorpha: rabbits research abstracts see: animals: chordata: vertebrates: mammals: lagomorpha: rabbits research

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FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 25000-9

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 22

MONTH: 06

YEAR: 2007

FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Keywords Mesh Terms:

KEYWORDS: Rabbits

MESH TERMS: metabolism

Chemical & Substance for Abstract: FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. Information

Substance Name: Adhesins, Bacterial

Registry Number: 0

Grant and Affiliation Information for FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells.

AFFILIATION: Department of Periodontics, Case Western Reserve University, Cleveland, Ohio 44106, USA.

Country: United States

AGENCY: United States NIDCR

GRANT: R01DE14924

ACRONYM: DE

MEDLINETA: J Biol Chem

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