Ship biofouling is one of the main vectors for the introduction and global spread of non-indigenous organisms. Diatoms
were the early colonizers of ship hulls; however, their community composition on ships is poorly understood. Herein, we
investigated the diatom community on the hull samples collected from two Korean research vessels Isabu (IRV) and Onnuri
(ORV) on September 2 and November 10, 2021, respectively. IRV showed low cell density (345 cells/cm2) compared to
ORV (778 cells/cm2). We morphologically identified more than 15 species of diatoms from the two research vessels (RVs).
The microalgae in both RVs were identified as Amphora, Cymbella, Caloneis, Halamphora, Navicula, Nitzschia, and Plagiogramma.
Of them, the genus Halamphora was found to be predominant. However, both RVs had a varied dominant
species with a significant difference in body size; Halamphora oceanica dominated at IRV, and Halamphora sp. at ORV,
respectively. Molecular cloning showed similar results to morphological analysis, in which Halamphora species dominated
in both RVs. The hull-attached species were distinct from species found in the water column. These results revealed diatoms
communities that are associated with ship hull-fouling at an early stage of biofilm formation. Moreover, ships arriving
from different regions could show some variation in species composition on their hull surfaces, with the potential for nonindigenous
species introduction.
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High-risk genotypes of human papillomaviruses (HPVs) are
directly implicated in various abnormalities associated with
cellular hyperproliferation, including cervical cancer. E6 is one
of two oncoproteins encoded in the HPV genome, which recruits
diverse PSD-95/Dlg/ZO-1 (PDZ) domain-containing
human proteins through its C-terminal PDZ-binding motif
(PBM) to be degraded by means of the proteasome pathway.
Among the three PDZ domain-containing protein tyrosine
phosphatases, protein tyrosine phosphatase non-receptor type
3 (PTPN3) and PTPN13 were identified to be recognized by
HPV E6 in a PBM-dependent manner. However, whether
HPV E6 associates with PTPN4, which also has a PDZ domain
and functions as an apoptosis regulator, remains undetermined.
Herein, we present structural and biochemical evidence
demonstrating the direct interaction between the PBM
of HPV16 E6 and the PDZ domain of human PTPN4 for the
first time. X-ray crystallographic structure determination and
binding measurements using isothermal titration calorimetry
demonstrated that hydrophobic interactions in which Leu158
of HPV16 E6 plays a key role and a network of intermolecular
hydrogen bonds sustain the complex formation between
PTPN4 PDZ and the PBM of HPV16 E6. In addition, it was
verified that the corresponding motifs from several other highrisk
HPV genotypes, including HPV18, HPV31, HPV33, and
HPV45, bind to PTPN4 PDZ with comparable affinities, suggesting
that PTPN4 is a common target of various pathogenic
HPV genotypes.
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