Novel structural patterns in divalent cation-depleted surface layers of Aeromonas salmonicida

Rafael A. Garduño; Barry M. Phipps; Wolfgang Baumeister; William W. Kay

doi:10.1016/1047-8477(92)90030-E

Novel structural patterns in divalent cation-depleted surface layers of Aeromonas salmonicida

Rafael A. Garduño, Barry M. Phipps, Wolfgang Baumeister, William W. Kay

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

Abstract

The fish pathogen Aeromonas salmonicida possesses a regular surface layer (or A-layer) which is an important virulence determinant. The A-protein, a single bilobed protein organized in a p4 lattice of M₄C₄ arrangement with two morphological domains, comprises this layer. The role of divalent cations in the A-layer structure was studied to better understand A-protein subunit interactions affecting structural flexibility and function. Divalent cation bridges were found to be involved in the integrity of the A-layer. Two novel A-layer patterns were formed as the result of growth under calcium limitation or by chelation of divalent cations with EDTA or EGTA, thereby constituting the first reported case of formation of distinct regular arrays upon divalent cation depletion. Furthermore, under these conditions A-protein was sometimes released as tetrameric units, rather than in monomeric form. The formation of the two novel patterns is best explained by a sequence of structural rearrangements, following disruption of only one of the two A-layer morphological units, that is, those held together by divalent cation bridges. The free tetrameric units represent four A-protein subunits clustered around the unaffected four-fold axis.

Original language	English
Pages (from-to)	184-195
Number of pages	12
Journal	Journal of Structural Biology
Volume	109
Issue number	3
DOIs	https://doi.org/10.1016/1047-8477(92)90030-E
Publication status	Published - 1992
Externally published	Yes

Bibliographical note

Funding Information:
We are grateful to J. L. Doran and J. Thornton for helpful advice. These studies were supported by a GREAT Award fellowship to R.A.G. from the Science Council of British Columbia, postdoctoral fellowship to B.M.P. from the Medical Research Council of Canada, and by grants to W.W.K. from the Natural Sciences and Engineering Research Council Canada (through the Centre for Bacterial Disease Research) from the British Columbia Health Care Research Foundation.

ASJC Scopus Subject Areas

Structural Biology

PubMed: MeSH publication types

Journal Article
Research Support, Non-U.S. Gov't

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10.1016/1047-8477(92)90030-E

Cite this

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title = "Novel structural patterns in divalent cation-depleted surface layers of Aeromonas salmonicida",

abstract = "The fish pathogen Aeromonas salmonicida possesses a regular surface layer (or A-layer) which is an important virulence determinant. The A-protein, a single bilobed protein organized in a p4 lattice of M4C4 arrangement with two morphological domains, comprises this layer. The role of divalent cations in the A-layer structure was studied to better understand A-protein subunit interactions affecting structural flexibility and function. Divalent cation bridges were found to be involved in the integrity of the A-layer. Two novel A-layer patterns were formed as the result of growth under calcium limitation or by chelation of divalent cations with EDTA or EGTA, thereby constituting the first reported case of formation of distinct regular arrays upon divalent cation depletion. Furthermore, under these conditions A-protein was sometimes released as tetrameric units, rather than in monomeric form. The formation of the two novel patterns is best explained by a sequence of structural rearrangements, following disruption of only one of the two A-layer morphological units, that is, those held together by divalent cation bridges. The free tetrameric units represent four A-protein subunits clustered around the unaffected four-fold axis.",

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note = "Funding Information: We are grateful to J. L. Doran and J. Thornton for helpful advice. These studies were supported by a GREAT Award fellowship to R.A.G. from the Science Council of British Columbia, postdoctoral fellowship to B.M.P. from the Medical Research Council of Canada, and by grants to W.W.K. from the Natural Sciences and Engineering Research Council Canada (through the Centre for Bacterial Disease Research) from the British Columbia Health Care Research Foundation.",

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AU - Baumeister, Wolfgang

AU - Kay, William W.

N1 - Funding Information: We are grateful to J. L. Doran and J. Thornton for helpful advice. These studies were supported by a GREAT Award fellowship to R.A.G. from the Science Council of British Columbia, postdoctoral fellowship to B.M.P. from the Medical Research Council of Canada, and by grants to W.W.K. from the Natural Sciences and Engineering Research Council Canada (through the Centre for Bacterial Disease Research) from the British Columbia Health Care Research Foundation.

PY - 1992

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N2 - The fish pathogen Aeromonas salmonicida possesses a regular surface layer (or A-layer) which is an important virulence determinant. The A-protein, a single bilobed protein organized in a p4 lattice of M4C4 arrangement with two morphological domains, comprises this layer. The role of divalent cations in the A-layer structure was studied to better understand A-protein subunit interactions affecting structural flexibility and function. Divalent cation bridges were found to be involved in the integrity of the A-layer. Two novel A-layer patterns were formed as the result of growth under calcium limitation or by chelation of divalent cations with EDTA or EGTA, thereby constituting the first reported case of formation of distinct regular arrays upon divalent cation depletion. Furthermore, under these conditions A-protein was sometimes released as tetrameric units, rather than in monomeric form. The formation of the two novel patterns is best explained by a sequence of structural rearrangements, following disruption of only one of the two A-layer morphological units, that is, those held together by divalent cation bridges. The free tetrameric units represent four A-protein subunits clustered around the unaffected four-fold axis.

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Novel structural patterns in divalent cation-depleted surface layers of Aeromonas salmonicida

Abstract

Bibliographical note

ASJC Scopus Subject Areas

PubMed: MeSH publication types

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