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Updated: Jan 20, 2026

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
Haloactinobacterium glacieicola sp. nov., isolated from an ice core
Feng Wang1,2, Yongqin Liu3,1,4, Ninglian Wang5,3
1University of Chinese Academy of Sciences, Beijing 100101, PR China.
Abstract:
A Gram-stain-positive, rod-shaped and motile bacterium with lateral flagellum, designated T3246-1T, was isolated from an ice core, which was drilled from Hariqin Glacier on the Tibetan Plateau, PR China. It grew optimally at 20 °C, pH 7-8 and in the presence of 3 % (w/v) NaCl. The major fatty acid of strain T3246-1T was anteiso-C15 : 0. Major polar lipids were diphosphatidylglycerol, phosphatidylglycerol and phosphatidylinositol. MK-8 was the dominant isoprenoid quinone. The whole-cell sugars were rhamnose, xylose and mannose. The major cell-wall peptidoglycan was lysine. The genomic DNA G+C content of the strain was 71.4 mol%. Results of phylogenetic analysis based on 16S rRNA gene sequences showed that strain T3246-1T formed a lineage within the genus Haloactinobacterium and was closely related to Haloactinobacterium album YIM 93306T with 95.99 % similarity. The average nucleotide identity value between strain T3246-1T and Haloactinobacterium album YIM 93306T was 76.65 %. Based on phenotypic and chemotaxonomic characteristics, strain T3246-1T was considered to represent a novel species of the genus Haloactinobacterium, for which the name Haloactinobacterium glacieicola sp. nov. is proposed. The type strain is T3246-1T (=CGMCC 1.13535T=JCM 32923T).
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