Cultivation, Detection, and Ecophysiology of Anaerobic Ammonium-Oxidizing Bacteria

Kartal, Boran; Geerts, Wim; Jetten, Mike S. M.

doi:10.1016/b978-0-12-381294-0.00004-3

Cited by 73 publications

(71 citation statements)

References 62 publications

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“…Anammox enrichment cultures contain about 80 to 95% anammox bacteria and are grown either as aggregates or as single cells in bioreactors, with very effective biomass retention (37,87,95). Their extremely long generation time is one of the reasons why they cannot be grown with standard microbial cultivation methods: they divide only once every 1 week (single cells) or 2 weeks (aggregated cells) under optimal conditions.…”

Section: Anammox Bacteriamentioning

confidence: 99%

Anaerobic Ammonium-Oxidizing Bacteria: Unique Microorganisms with Exceptional Properties

Niftrik

Jetten

2012

Microbiol Mol Biol Rev

232

103

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SUMMARY Anaerobic ammonium-oxidizing (anammox) bacteria defy many microbiological concepts and share numerous properties with both eukaryotes and archaea. Among their most intriguing characteristics are their compartmentalized cell plan and archaeon-like cell wall. Here we review our current knowledge about anammox cell biology. The anammox cell is divided into three separate compartments by bilayer membranes. The anammox cell consists of (from outside to inside) the cell wall, paryphoplasm, riboplasm, and anammoxosome. Not much is known about the composition or function of both the anammox cell wall and the paryphoplasm compartment. The cell wall is proposed to be proteinaceous and to lack both peptidoglycan and an outer membrane typical of Gram-negative bacteria. The function of the paryphoplasm is unknown, but it contains the cell division ring. The riboplasm resembles the standard cytoplasmic compartment of other bacteria; it contains ribosomes and the nucleoid. The anammoxosome occupies most of the cell volume and is a so-called “prokaryotic organelle” analogous to the eukaryotic mitochondrion. This is the site where the anammox reaction takes place, coupled over the curved anammoxosome membrane, possibly giving rise to a proton motive force and subsequent ATP synthesis. With these unique properties, anammox bacteria are food for thought concerning the early evolution of the domains Bacteria , Archaea , and Eukarya .

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Section: Anammox Bacteriamentioning

confidence: 99%

Anaerobic Ammonium-Oxidizing Bacteria: Unique Microorganisms with Exceptional Properties

Niftrik

Jetten

2012

Microbiol Mol Biol Rev

232

103

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“…Cells were harvested from a "Ca. Kuenenia stuttgartiensis" single-cell membrane bioreactor at an optical density at 600 nm (OD 600 ) of 1.1 and were centrifuged for 10 min at 4,000 ϫ g to concentrate them 40-fold in their original growth medium (35). Cells were then stored at Ϫ80°C and thawed just before the S-layer enrichment procedure.…”

Section: Methodsmentioning

confidence: 99%

A New Addition to the Cell Plan of Anammox Bacteria: "Candidatus Kuenenia stuttgartiensis" Has a Protein Surface Layer as the Outermost Layer of the Cell

Teeseling¹,

Almeida²,

Klingl³

et al. 2013

Journal of Bacteriology

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bAnammox bacteria perform anaerobic ammonium oxidation (anammox) and have a unique compartmentalized cell consisting of three membrane-bound compartments (from inside outwards): the anammoxosome, riboplasm, and paryphoplasm. The cell envelope of anammox bacteria has been proposed to deviate from typical bacterial cell envelopes by lacking both peptidoglycan and a typical outer membrane. However, the composition of the anammox cell envelope is presently unknown. Here, we investigated the outermost layer of the anammox cell and identified a proteinaceous surface layer (S-layer) (a crystalline array of protein subunits) as the outermost component of the cell envelope of the anammox bacterium "Candidatus Kuenenia stuttgartiensis." This is the first description of an S-layer in the phylum of the Planctomycetes and a new addition to the cell plan of anammox bacteria. This S-layer showed hexagonal symmetry with a unit cell consisting of six protein subunits. The enrichment of the S-layer from the cell led to a 160-kDa candidate protein, Kustd1514, which has no homology to any known protein. This protein is present in a glycosylated form. Antibodies were generated against the glycoprotein and used for immunogold localization. The antiserum localized Kustd1514 to the S-layer and thus verified that this protein forms the "Ca. Kuenenia stuttgartiensis" S-layer.

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“…This reaction is followed by the oxidation of hydrazine to N 2 (equation 3), which is catalyzed by hydrazine dehydrogenase (HDH; kustc0694), an enzyme that is related to hydroxylamine oxidoreductase (HAO) of aerobic ammonium-oxidizing bacteria (1). The electrons released from this reaction (equation 3) ultimately are used to drive the first two reductive steps (equations 1 and 2).…”

mentioning

confidence: 99%

Immunogold Localization of Key Metabolic Enzymes in the Anammoxosome and on the Tubule-Like Structures of Kuenenia stuttgartiensis

et al. 2015

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Anaerobic ammonium-oxidizing (anammox) bacteria oxidize ammonium with nitrite as the terminal electron acceptor to form dinitrogen gas in the absence of oxygen. Anammox bacteria have a compartmentalized cell plan with a central membrane-bound "prokaryotic organelle" called the anammoxosome. The anammoxosome occupies most of the cell volume, has a curved membrane, and contains conspicuous tubule-like structures of unknown identity and function. It was suggested previously that the catalytic reactions of the anammox pathway occur in the anammoxosome, and that proton motive force was established across its membrane. Here, we used antibodies raised against five key enzymes of the anammox catabolism to determine their cellular location. The antibodies were raised against purified native hydroxylamine oxidoreductase-like protein kustc0458 with its redox partner kustc0457, hydrazine dehydrogenase (HDH; kustc0694), hydroxylamine oxidase (HOX; kustc1061), nitrite oxidoreductase (NXR; kustd1700/03/04), and hydrazine synthase (HZS; kuste2859-61) of the anammox bacterium Kuenenia stuttgartiensis. We determined that all five protein complexes were exclusively located inside the anammoxosome matrix. Four of the protein complexes did not appear to form higher-order protein organizations. However, the present data indicated for the first time that NXR is part of the tubule-like structures, which may stretch the whole length of the anammoxosome. These findings support the anammoxosome as the locus of catabolic reactions of the anammox pathway. IMPORTANCEAnammox bacteria are environmentally relevant microorganisms that contribute significantly to the release of fixed nitrogen in nature. Furthermore, the anammox process is applied for nitrogen removal from wastewater as an environment-friendly and cost-effective technology. These microorganisms feature a unique cellular organelle, the anammoxosome, which was proposed to contain the energy metabolism of the cell and tubule-like structures with hitherto unknown function. Here, we purified five native enzymes catalyzing key reactions in the anammox metabolism and raised antibodies against these in order to localize them within the cell. We showed that all enzymes were located within the anammoxosome, and nitrite oxidoreductase was located exclusively at the tubule-like structures, providing the first insights into the function of these subcellular structures.

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Cultivation, Detection, and Ecophysiology of Anaerobic Ammonium-Oxidizing Bacteria

Cited by 73 publications

References 62 publications

Anaerobic Ammonium-Oxidizing Bacteria: Unique Microorganisms with Exceptional Properties

Anaerobic Ammonium-Oxidizing Bacteria: Unique Microorganisms with Exceptional Properties

A New Addition to the Cell Plan of Anammox Bacteria: "Candidatus Kuenenia stuttgartiensis" Has a Protein Surface Layer as the Outermost Layer of the Cell

Immunogold Localization of Key Metabolic Enzymes in the Anammoxosome and on the Tubule-Like Structures of Kuenenia stuttgartiensis

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