The interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaalpha2,3Gal glycosidic linkage over those with Siaalpha2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin.

Recently, we found that Alcanivorax bacteria from various marine environments were capable of degrading halogenated alkanes. Genome sequencing of A. dieselolei B-5 revealed two putative haloalkane dehalogenase (HLD) genes, which were supposed to be involved in degradation of halogenated compounds. In this report, we confirm for the first time that the Alcanivorax bacterium encodes a truly functional HLD named DadB. An activity assay with 46 halogenated substrates indicated that DadB possesses broad substrate range and has the highest overall activity among the identified HLDs. DadB prefers brominated substrates; chlorinated alkenes; and the C2-C3 substrates, including the persistent pollutants of 1,2-dichloroethane, 1,2-dichloropropane and 1,2,3-trichloropropane. As DadB displays no detectable activity toward long-chain haloalkanes such as 1-chlorohexadecane and 1-chlorooctadecane, the degradation of them in A. dieselolei B-5 might be attributed to other enzymes. Kinetic constants were determined with 6 substrates. DadB has highest affinity and largest k cat/K m value toward 1,3-dibromopropane (K m = 0.82 mM, k cat/K m = 16.43 mM−1·s−1). DadB aggregates fast in the buffers with pH≤7.0, while keeps stable in monomer form when pH≥7.5. According to homology modeling, DadB has an open active cavity with a large access tunnel, which is supposed important for larger molecules as opposed to C2-C3 substrates. Combined with the results for other HLDs, we deduce that residue I247 plays an important role in substrate selection. These results suggest that DadB and its host, A. dieselolei B-5, are of potential use for biocatalysis and bioremediation applications.

Methicillin-resistant Staphylococcus aureus (MRSA) is a serious and rapidly growing threat to human beings. Emodin has a potent activity against MRSA; however, its usage is limited due to high hydrophobicity and low oral bioavailability. Thus, the coaxial electrospinning nanofibers encapsulating emodin in the core of hydrophilic poly (vinylpyrrolidone), with a hygroscopic cellulose acetate sheath, have been fabricated to provide long-term effect against MRSA. Scanning electron microscopy and transmission electron microscopy confirmed the nanofibers had a linear morphology with nanometer in diameter, smooth surface, and core-shell structure. Attenuated total reflection-Fourier transform infrared spectra, X-ray diffraction patterns, and differential scanning calorimetric analyses verified emodin existed in amorphous form in the nanofibers. The nanofibers have 99.38 ± 1.00% entrapment efficiency of emodin and 167.8 ± 0.20% swelling ratio. Emodin released from nanofibers showed a biphasic drug release profile with an initial rapid release followed by a slower sustained release. CCK-8 assays confirmed the nontoxic nature of the emodin-loaded nanofibers to HaCaT cells. The anti-MRSA activity of the nanofibers can persist up to 9 days in AATCC147 and soft-agar overlay assays. These findings suggest that the emodin-loaded electrospun nanofibers with core-shell structure could be used as topical drug delivery system for wound infected by MRSA.

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A Gram-stain-negative, strictly aerobic, yellow-pigmented, non-gliding, oval to rod-shaped bacterial strain, designated JB01H24, belonging to the family Flavobacteriaceae, was isolated from marine surface sediment collected from the Ross Sea, Antarctica. Strain JB01H24 grew at 4-40 °C (optimum 25-30 °C), pH 7.0-9.0 (optimum 7.5-8.0), and in the presence of 0-8 % NaCl (optimum 3 %, w/v). Phylogenetic analysis based on 16S rRNA gene sequences showed that strain JB01H24 formed an independent linkage within the family Flavobacteriaceae and was closely related with the genus Gillisia. Strain JB01H24 exhibited 16S rRNA gene sequence similarities of 95.3-91.5 % and 94.9-94.0 % to the type strains of the genera Gillisia and Salinimicrobium, respectively. The major fatty acids (>5 %) were iso-C15 : 0, summed feature 3 (C16 : 1ω6c and/or C16 : 1ω7c), anteiso-C15 : 0, iso-C15 : 1 G and summed feature 9 (iso-C17 : 1ω9c and/or 10-methyl C16 : 0). The major polar lipids were phosphatidylethanolamine, seven unidentified lipids, two unidentified aminolipids and an unidentified aminophospholipid. Strain JB01H24 contained menaquinone-6 as the only ubiquinone. The DNA G+C content was 42.4 mol%. On the basis of phylogenetic, physiological and chemotaxonomic properties, strain JB01H24 is considered to represent a novel species of a new genus within the family Flavobacteriaceae, for which the name Antarcticibacterium flavum gen. nov., sp. nov. is proposed. The type strain of Antarcticibacterium flavum is JB01H24 (=GDMCC 1.1229=KCTC 52984).

Saccharomyces cerevisiae is increasingly being used for the production of chemicals derived from acetyl coenzyme A (acetyl-CoA). However, the inadequate supply of cytosolic acetyl-CoA often leads to low yields. Here, we developed a novel strategy for balancing acetyl-CoA metabolism and increasing the amount of the downstream product. First, the combination of acetaldehyde dehydrogenase (eutE) and acetoacetyl-CoA thiolase (AtoB) was optimized to redirect the acetyl-CoA flux toward the target pathway, with a 21-fold improvement in mevalonic acid production. Second, pathway engineering and evolutionary engineering were conducted to attenuate the growth deficiency, and a 10-fold improvement of the maximum productivity was achieved. Third, acetyl-CoA carboxylase (ACC1) was dynamically downregulated as the complementary acetyl-CoA pathway, and the yield was improved more than twofold. Fourth, the most efficient and complementary acetyl-CoA pathways were combined, and the final strain produced 68 mg/g CDW lycopene, which was among the highest yields reported in S. cerevisiae. This study demonstrates a new method of producing lycopene products by regulating acetyl-CoA metabolism.

The benthic bacterial community in Antarctic continental shelf ecosystems are not well-documented. We collected 13 surface sediments from the Ross Sea, a biological hotspot in high-latitude maritime Antarctica undergoing rapid climate change and possible microflora shift, and aimed to study the diversity, structure and assembly mechanism of benthic bacterial community using both culture-dependent and -independent approaches. High-throughput sequencing of 16S rRNA gene amplicons revealed 370 OTUs distributed in 21 phyla and 284 genera. The bacterial community was dominated by Bacteroidetes, Gamma- and Alphaproteobacteria, and constituted by a compact, conserved and positively-correlated group of anaerobes and other competitive aerobic chemoheterotrophs. Null-model test based on βNTI and RCBray indicated that stochastic processes, including dispersal limitation and undominated fractions, were the main forces driving community assembly. On the other hand, environmental factors, mainly temperature, organic matter and chlorophyll, were significantly correlated with bacterial richness, diversity and community structure. Moreover, metabolic and physiological features of the prokaryotic taxa were mapped to evaluate the adaptive mechanisms and functional composition of the benthic bacterial community. Our study is helpful to understand the structural and functional aspects, as well as the ecological and biogeochemical role of the benthic bacterial community in the Ross Sea.

The complete 16S rRNA gene sequence and draft genome of Marinobacter denitrificans JB02H27 T have been deposited in GenBank under accession numbers MN203987 and VMHN00000000, respectively. The draft genome sequences of Marinobacter confluentis KCTC 42705 T and Marinobacter halotolerans NBRC 110910 T have been deposited in GenBank under accession numbers VMHO00000000 and VMHP00000000, respectively. †These authors contributed equally to this work One supplementary table and three supplementary figures are available with the online version of this article.