Direct comparison of antibody responses to four SARS-CoV-2 vaccines in Mongolia.

Different SARS-CoV-2 vaccines are approved in various countries, but few direct comparisons of the antibody responses they stimulate have been reported. We collected plasma specimens in July 2021 from 196 Mongolian participants fully vaccinated with one of four COVID-19 vaccines: Pfizer/BioNTech, AstraZeneca, Sputnik V, and Sinopharm. Functional antibody testing with a panel of nine SARS-CoV-2 viral variant receptor binding domain (RBD) proteins revealed marked differences in vaccine responses, with low antibody levels and RBD-ACE2 blocking activity stimulated by the Sinopharm and Sputnik V vaccines in comparison to the AstraZeneca or Pfizer/BioNTech vaccines. The Alpha variant caused 97% of infections in Mongolia in June and early July 2021. Individuals who recover from SARS-CoV-2 infection after vaccination achieve high antibody titers in most cases. These data suggest that public health interventions such as vaccine boosting, potentially with more potent vaccine types, may be needed to control COVID-19 in Mongolia and worldwide.

Bacillus licheniformis α-amylase: Structural feature in a biomimetic solution and structural changes in extrinsic conditions.

Bacillus licheniformis α-amylase (BLA) in a biomimetic buffer and extrinsic solutions (various pH values, temperatures, and metal ions) has been investigated for the first time in the view of three-dimensional (3D) structure by synchrotron X-ray and dynamic light scattering analyses. BLA in buffer is determined to have a structure resembling its crystallographic structure; but the 3D structure is slightly larger than the crystal structure. Such a structure is maintained with little variations in extrinsic solutions of pH 4.0-9.7, temperature 4-55 °C, and metal ions such as Ba2+, Mg2+, and Li+. These results collectively inform that BLA tends to favorably form a stable monomeric structure, which could provide structural clues to its enzymatic activities in moderate levels. Interestingly, BLA is found to reveal highly expanded structures at 65-75 °C and in Co2+ solution, which could correlate to the significantly pronounced enzymatic activities. However, BLA shows somewhat shrunken structures at pH 3.0 and in Hg2+ solution, supporting for the suppressed activities under these conditions.

Structural Characteristics of Pneumolysin and Its Domains in a Biomimetic Solution.

Pneumolysin (PLY) and its truncated fragments, domains 1-3 (D1-3), and domain 4 (D4), were purified as recombinant proteins after being cloned and over-expressed in Escherichia coli. The three-dimensional structures of these proteins were quantitatively investigated in a biomimetic condition, phosphate buffered saline (PBS) by synchrotron X-ray scattering. X-ray scattering analysis revealed important structural features including structural parameters. PLY was present as a monomeric form in PBS. The monomeric form resembled its crystallographic structure with a discrepancy of only 6.3%, confirming that PLY forms a stable structure and, thus, retains its structure in the crystalline state and even in PBS solution. D4 was also present as a monomeric form, but its structure was very different from that of the corresponding part in the crystallographic PLY structure; the discrepancy was 92.0%. Such a dissimilar structure might originate from a less folded-chain conformation. This result suggested that the structure of D4 is highly dependent on the crystalline or solution state and further on the presence or absence of the D1-3 unit. In contrast, D1-3 was dimeric rather than monomeric. Its structure was close to the most probable dimeric form of the corresponding part in the crystallographic PLY structure with 13.1% discrepancy. This fact indicated that the D1-3 unit forms a stable structure and, indeed, such structure is well maintained in the crystalline state as well as in PBS although presented as a dimer. This result further supported that the whole structural stability of PLY is mainly attributed to the structure of D1-3. All of PLY, D1-3, and D4 revealed aggregation tendencies during purification and storage. Overall, the structural characteristics of PLY and its domains in PBS may correlate to the PLY oligomer formation yielding large pore structures for the penetration of cell membranes.