Glycobiology, 2019, vol. 29, no.

6, 461–468
doi: 10.1093/glycob/cwz013
Advance Access Publication Date: 26 March 2019
Glyco-Informatics

Microbial Biology

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ProGlycProt V2.0, a repository of experimentally
validated glycoproteins and protein
glycosyltransferases of prokaryotes
Pravinkumar Choudhary, Rupa Nagar, Vaidhvi Singh,
Aadil Hussain Bhat, Yogita Sharma, and Alka Rao1
CSIR-Institute of Microbial Technology, Sector 39 A, Chandigarh 160036, India
1
To whom correspondence should be addressed: e-mail: raoalka@imtech.res.in
Received 24 October 2018; Revised 22 February 2019; Editorial decision 24 February 2019; Accepted 1 March 2019

Abstract
Knowledge of glycosylation status and glycan-pattern of proteins are of considerable medical, aca-
demic and application interest. ProGlycProt V2.0 (www.proglycprot.org) therefore, is conceived
and maintained as an exclusive web-resource providing comprehensive information on experi-
mentally validated glycoproteins and protein glycosyltransferases (GTs) of prokaryotic origin. The
second release of ProGlycProt features a major update with a 191% increase in the total number
of entries, manually collected and curated from 607 peer-reviewed publications, on the subject.
Protein GTs from prokaryotes that catalyze a varied range of glycan linkages are amenable gly-
coengineering tools. Therefore, the second release presents content that is greatly expanded and
reorganized in two sub-databases: ProGPdb and ProGTdb. While ProGPdb provides information
about validated glycoproteins (222 entries), ProGTdb catalogs enzymes/proteins that are instru-
mental in protein glycosylation, directly (122) or as accessory proteins (182). ProGlycProt V2.0
remains highly cross-referenced yet exclusive and complementary in content to other related data-
bases. The second release further features enhanced search capability, a “compare” entries
option and an innovative geoanalytical tool (MapView) facilitating location-assisted search-cum fil-
tering of the entries using geo-positioning information of researchers/groups cited in the
ProGlycProt V2.0 databases. Thus, ProGlycProt V2.0 continues to serve as a useful one-point web-
resource on various evidence-based information on protein glycosylation in prokaryotes.

Key words: archaea, bacteria, glycosyltransferase, prokaryotic glycoproteins, protein glycosylation

Introduction adhesion, host colonization, immune modulation or evasion in pro-

The enzymatic process of attachment of sugar moiety (glycan) on
to a specific residue (glycosite) in a protein (now termed glycopro-
tein) is known as protein glycosylation. This is a co/post-transla-
tional modification (PTM) event. The enzymes involved in glycan
transfer on to the proteins are called glycosyltransferases (GTs).
Glycoproteins thus synthesized serve a variety of important func-
tions in a cell including folding, stability, and targeting of proteins,
interactions between cells, and regulation of signal transduction and
host immune responses in eukaryotes and pathogenicity, motility,
karyote (Lepenies and Seeberger 2014) (Eichler and Koomey 2017).
While protein glycosylation is the most abundant PTM and fairly
well understood in eukaryotes, extent, and spectrum of protein gly-
cosylation in prokaryotes is still in the exploration phase (Schaffer
and Messner 2017). However, and since the discovery of the first
glycoprotein in S-layer of archaea Halobacterium halobium in 1974,
all the early findings and ongoing research in protein glycosylation
in prokaryotes is full of surprises (Latousakis and Juge 2018).
Indeed, beginning with the first general protein glycosylation system

© The Author(s) 2019. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 461
462
identified in Campylobacter jejuni in 1999 (Szymanski et al. 1999),
a bouquet of glycosylation mechanisms are now known in bacteria
and archaea that include but are not limited to two classic (eukary-
otic) glycosylation systems, namely en bloc N-glycosylation and
sequential O-glycosylation (Keys and Aebi 2017) (Li et al. 2017).
Befitting is an amazing diversity of glycans in terms of nature, type,
and number in prokaryotic glycoproteins (Bhat et al. 2011) (Herget
et al. 2008). Appropriately again, the range of glycosyltransferases
flaunting hitherto unknown specificities and catalyzing yet newer lin-
kages is indeed impressive in prokaryotes (Latousakis and Juge 2018).
One example is recently discovered protein S-glycosylation in bacteria,
wherein glycan is attached to Cys residue in antimicrobial peptides of
the bacteria (Norris and Patchett 2016). Similarly, ApHMW1C/
ApNGT catalyzes cytoplasmic and sequential N-glycosylation of adhe-
sion protein in Actinobacillus pleuropneumoniae (ApNGT). Successful
functional transfer of this system into Escherichia coli, further revealed
that ApNGT has a relaxed substrate specificity and is capable of both
N- and O-linked glycosylation (Naegeli et al. 2014). Such enzymes exhi-
biting relaxed specificity with respect to protein–glycan linkages are
indeed unique to bacteria, at present.
For the reasons that the majority of therapeutic proteins/peptides
are glycoproteins and many successful current-age vaccines are gly-
coconjugates (Cuccui and Wren 2015) (Sethuraman and Stadheim
2006), prokaryotic glycosylation systems and enzymes are of
immense application value and well exemplified by ongoing glycoen-
gineering efforts (Xu et al. 2017) (Ogura et al. 2016) and steadily
growing patent landscape and research publications in this field
(Supplementary Data, Figure 1 & 2 and Table SI). However, experi-
mental details of these enzymes and their substrates are not readily
available or schematically cataloged at one point for the easy
retrieval. It is pertinent to mention here that while universal protein
databases like UniProt, SwissProt, universal carbohydrate databases
like UniCarb-DB (Hayes et al. 2011), and universal glycosyltransfer-
ase enzyme databases like Carbohydrate-Active enZYmes (CAZy)
(Lombard et al. 2013) are rich source of general information, retriev-
ing domain specific, organism-specific or application specific informa-
tion from these databases is either not available or is often manually
intensive and not user-friendly. Therefore, many specific databases
have been developed to cater to such usage. For example, databases
like VSGdb (Marcello et al. 2007), GlycoProtDB (Kaji et al. 2017),
GlycoFish (Baycin-Hizal et al. 2011a), GlycoFly (Baycin-Hiza et al.
2011b), etc. are the organism-specific databases of trypanosomal vari-
ant surface glycoproteins, N-linked glycoproteins of C. elegans,
Zebrafish and Drosophila, respectively. Further, in this context, rele-
vance and importance of domain and organism-specific GT databases
is well introduced in a recently published GT database, namely
CSDB_GT for model plant A. thaliana (Egorova and Toukach 2017).
Therefore, while the first release of ProGlycProt (Bhat et al.
2011) served as an exclusive web-resource providing information on
experimentally validated glycoproteins of prokaryotes, the updated
ProGlycProt V2.0 provides a web resource for both glycoproteins
and protein glycosyltransferases that are validated by scientific pub-
lished experiments, in prokaryotes. Additionally, we have provided
a new and intuitive web interface to access the data. We expect this
updated database to be more useful for the scientific community, in
particular for glycobiologists interested in protein glycosylation
using prokaryotic systems or applications of prokaryotic glycopro-
teins. ProGlycProt second release is updated in quality as well as
quantity (Supplementary Data, Table SII and SIII) so as to cater to
both academic and application interests of the broader scientific
community. The second release not only provides current estimates
P Choudhary et al.
of the extent of protein glycosylation and diversity of protein-linked
glycans observed in prokaryotes but also the detailed, searchable
catalog of prokaryotic protein glycosyltransferases (ProGTdb) for
which at least one published experimental evidence is available. One
of the important features of the second release is the introduction of
a new geoanalytical tool, “MapView” whereby database entries can
be searched using location preferences.
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Results and discussion
The second release of ProGlycProt presents a 191% increase in the
total number of entries, manually collected and curated from 607
peer-reviewed publications on the subject. The content is further
reorganized in two sub-databases: ProGPdb and ProGTdb. While
ProGPdb provides information about validated glycoproteins (222
entries), ProGTdb catalogs enzymes/proteins that are instrumental
in protein glycosylation, directly (122) or as accessory proteins
(182) and miscellaneous experimental information covering various
aspects of protein glycosylation in prokaryotes. An estimate of value
addition through manual annotation in quality and quantity in the
information available at ProGlycProt V2.0 vis-à-vis other related
and or cross-linked databases like UniProt, CAZy, GlyTouCan and
BCSDB is given in Supplementary Data, Table SIV.
In this context, ProGTdb catalogs GTs unique to bacteria that
catalyze cytoplasmic and sequential N-glycosylation (ApNGT)
in Actinobacillus pleuropneumoniae (ProGT42) and S-glycosylation.
The extracellular S-glycosylated (antimicrobial) peptides namely
Glycocin F and Sublancin 168 in Lactobacillus plantarum KW30 and
Bacillus subtilis 168, respectively are discovered almost at the same
time in 2011 (Oman et al. 2011) (Stepper et al. 2011). Subsequently,
the protein SunS (ProGT46 (SunS)) was identified as the enzyme
instrumental in catalyzing S-linkage in the bacterial cytoplasm. Thus,
glycosylated Sublancin is then exported out by dedicated transporters
in B. subtilis. However, ThuS from Bacillus thuringiensis serovar
andalousiensis BGSC 4AW1 (ProGT65 (ThuS)), a close homolog of
SunS turns out both an O- and S-glycosyltransferase, later on. ThuS is
capable of transferring a monosaccharide on to Ser/Thr and Cys resi-
dues in the acceptor peptide (Wang et al. 2014). In this league, the
most recent addition is EntS, an O- and S-glycosyltransferase from
Enterococcus faecalis TX0104 (ProGT116 (EntS)). While SunS and
ThuS can transfer monosaccharides on to acceptor residue, EntS can
transfer two monosaccharides in a sequential and iterative fashion on
to the acceptor peptide (Nagar and Rao 2017). Further, while out of
191 characterized GTs described in ProGTdb, 36 entries are unique to
ProGTdb, whereas 40 entries in ProGTdb correspond to an acceptor
substrate of GT that is either a synthetic peptide or a eukaryotic pro-
tein (e.g., ProGT89 (CcPglB), ProGT63 (NleB1) and ProGT64
(TcsH)). ProGTdb additionally catalogs in vitro engineered/evolved
variants of the GT’s that are not available in any of the universal pro-
tein databases (e.g., ProGT10 (PglB) and ProGT47 (ClPglB)).
Similarly, 15 entries represent glycosyltransferases that glycosylate
eukaryotic proteins such as RhoA, Rac1, Ras and EF1A that are
mostly involved in signaling pathways (e.g., ProGT81 (TcnA) and
ProGT45 (TpeL)).
Based on current experimental data, the maximum entries in
ProGlycProt V2.0 belong to bacteria namely Firmicutes (32%) and
Proteobacteria (53%) (Figure 4A and B). In Firmicutes all GT’s cata-
lyze O- (Ser/Thr/Tyr) and/or S- (Cys) linked glycosylation but in
case of Proteobacteria both N- (Arg/Asn) linked and O- (Ser/Thr/
Tyr) linked glycosylation is present (Figure 4C). While GTs involved
in en bloc transfer (44% of the total entries) belong to GT66 family,
ProGlycProt V2.0, a repository of glycoproteins and protein glycosyltransferases
Fig. 1. Schema representing the overall design, features, and functioning of the ProGlycProt V2.0 web-resource.
largely (Figure 4D), GT’s transferring glycan sequentially (56%
total) are widely spread in different families such as GT88, GT44,
GT41, GT4, GT39, GT2, GT104, GT8 (Figure 4E).
A large number of entries (79% of the total) belong to patho-
genic bacteria (e.g., ProGT106 (SseK3), Figure 4F) which may not
necessarily mean that glycosylation is more important in pathogenic
viz non-pathogenic bacteria but that understanding of pathogenesis
is a priority research area and glycosylation does play a role in the
life cycle of pathogenic bacteria.
Akin to protein O-GlcNAcylation in eukaryotes, in bacteria also as
many as 17 GTs are described that are involved in the sequential trans-
fer of GlcNAc (e.g., ProGT20 (GmaR)) albeit with different biological
and physiological relevance of the aforementioned modification.
In Map View Tool, a total of 2045 corresponding authors have
been mapped/geotagged corresponding to the published literature.
Among geotagged authors, 1474 are cited under ProGPdb, 389
under ProGT_Main and 182 under ProGT_Accessory.
Accordingly, ProGlycProt V2.0 remains the largest collection of
evidence-based information on prokaryotic glycoproteins, glycosites
and corresponding glycosyltransferases. It is highly cross-referenced
yet non-redundant exclusive database in terms of information pro-
vided vis-à-vis universal protein databases, glycan databases and
463
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glycosyltransferase databases as listed in Supplementary Data,
Table SII & SV. ProGlycProt V2.0 also is a registered partner website
of GlyTouCan – the universal glycan structure repository. Knowing
that prokaryotic glycosites are often very different from eukaryotic
glycoproteins, the information on 635 experimentally verified glyco-
sites further may serve as a ready resource for the training and opti-
mization of prokaryotic glycosite prediction tools (Supplementary
Data, Table SII and SIII) (Chauhan et al. 2012) or to design innovative
cell-based or in vitro glycoengineering and glycodiversification experi-
ments. In a similar spirit, we envision all future updates of
ProGlycProt V2.0 shall be incorporating deeper details on transla-
tional experiments and IPR information (Supplementary Data,
Table SI) and on the application of prokaryotic glycosylation systems.
Material and methods
Data collection and curation
The data entries and information compiled under ProGlycProt V2.0
is retrieved manually from various forms of peer-reviewed literature
and subsequent references cited within and as obtained from
PubMed, Google Scholar and the Web of Science using various key-
words that are mentioned under the Supplementary materials. The
464 P Choudhary et al.

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Fig. 2. ProGlycProt V2.0 entity-relationship (ER) diagram. The main entities of the database namely ProGPdb and ProGTdb are represented in bold square shape
box (yellow) and (orange), respectively. Solid arrows indicate data flow in ProGlycProt V2.0, while dashed arrows indicate a connection to the external database.
Tables (cyan) are connected by a solid arrow indicating they are directly associated with ProGlycProt V2.0 and ultimately leads to ProGP ID/ProGT ID. PK is the
primary key and FK is a foreign key.

second release presents information compiled from 519 research
papers and 88 review articles, in total. The data is also curated on
account of removing duplicity in records under different queries or to
reflect the latest finding or even contradictory finding, if any. The
mutated/glycoengineered or non-native prokaryotic glycoproteins or
acceptor protein/peptides are also included in the additional informa-
tion and in acceptor substrate information column in ProGPdb or
ProGTdb against relevant entries (e.g., ProGP347 (spermidine/putres-
cine binding protein), ProGT42 (ApNGT), ProGT116 (EntS)).
Similarly, glucosyltransferase toxins as in Legionella pneumophila and
Photorhabdus asymbiotica, glycosylate Ser/Thr or Tyr residues of
human (host) proteins, namely elongation factor 1 A (eEF1A) and
Rho GTPase. The information of such eukaryotic/non-bacterial sub-
strate proteins is included under acceptor substrate field of the
ProGTdb database (e.g., ProGT2-7, ProGT19 (Lgt), ProGT27 (Lgt),
ProGT28 (Lgt), ProGT68 (PaTox)). The overall quantitative and
qualitative measures of updates in content, features, design and sche-
ma of the web-resource ProGlycProt V2.0 are represented in Figure 1.
Data arrangement
In the second release of the ProGlycProt, the information is arranged
under two sub-databases namely, ProGPdb and ProGTdb.
ProGPdb
Is the compilation of experimentally verified glycoproteins of
archaeal and bacterial origin under two sections: ProCGP and
ProUGP. While ProUGP section provides information about
ProGlycProt V2.0, a repository of glycoproteins and protein glycosyltransferases
Fig. 3. Sorting of data entries based on different classifiers under “Search by feature” option and its search outcome.
proteins for which experimental evidence of glycosylation is avail-
able, the ProCGP section provides information about glycoproteins
wherein at least one site of glycosylation is known. In the second
release, the primary information schema, data fields and subfields of
the original ProGlycProt database have been retained as ProGPdb
with following improvizations (Bhat et al. 2011):
Each entry in ProGPdb has a unique ProGP ID defined in the
chronological-alphabetic order. The extent of cross-referencing is
increased by linking each entry with current and relevant repositor-
ies like GlyTouCan (Tiemeyer et al. 2017). Further, in second release
several ProUGP entries are updated in terms of minor information
spread across various fields and seven of them are upgraded as
ProCGP by adding information on annotated glycosites and related
evidence, literature, etc.
ProGTdb
Is the compilation of proteins/enzymes that are involved in N-, O- and
S-glycosylation of proteins in prokaryotes and for which at least one
experimental (biochemical/genetic) evidence is available in the pub-
lished literature. ProGTdb is further arranged in two sections namely;
ProGT_Main and ProGT_Accessory. The section ProGT_Main con-
tains information about enzymes that are involved directly in the
transfer of glycan on to the peptide/polypeptide. Whereas the
section ProGT_Accessory provides information about proteins that
have an additional/associated function like glycan assembly on lipid
moiety, glycan flipping over the membrane, glycan extension, glycan
modification, etc. in a given protein glycosylation pathway. Pictorial
representations depicting glycosylation pathways are provided in cases
where primary protein glycosyltransferase(s) and all or some of its
accessory enzymes/GT’s responsible for glycan formation/transfer are
known in the literature e.g., ProGT1 (PilO), ProGT18 (PseD) and
ProGT9 (PglB). Briefly, ProGTdb contains information about the
native organism, genome, gene, protein, detailed description of the
acceptor and donor substrate specificity, linkage(s) catalyzed,
465
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mechanism of glycan transfer, protein structure, evidence of biochem-
ical and/or genetic characterization of the glycosyltransferase activity
of the enzyme, literature and additional information. Entire informa-
tion in ProGTdb is organized under nine broad fields and 355 sub-
fields that are searchable by a variety of criteria. A detailed
description of each broad field is provided in the supplementary text.
Entries in ProGTdb are cross-referenced to corresponding substrate
proteins in ProGPdb and vice versa. Further, the contents in ProGTdb
are largely non-overlapping (rather complementary) to contents avail-
able at CAZy (http://www.cazy.org/GlycosylTransferases.html) as
entries in ProGT_Main are curated with extensive information includ-
ing biochemical/genetic evidence of catalytic activity, linkage cata-
lyzed, glycan transferred, methods, functional significance, mutant/
engineered variants, detailed information on donor/acceptor sub-
strates and specificities thereof as well as equally extensive informa-
tion about associated proteins/enzyme of an experimentally validated
glycosylation pathway in prokaryotes.
Other updates and new additions
In addition to quantitative aspects defined in Supplementary Data,
Table SII and as expected with an increase in number of entries, the
second release indeed has a significantly better representation
(Supplementary Data, Figure S3) of various prokaryotic genus in
comparison to the first release of ProGlycProt (Bhat et al. 2011).
While most of the existing useful features like number of Search and
Display criteria, options like Download Results, Print Results,
submit your Glycoprotein/Enzyme form, glycoprotein sequence ana-
lysis tools namely, MapSequon, GlySeq Extractor, BLAST, Structure
Gallery and Links are retained with necessary content updates in
databases (Supplementary Data, Table SII & SIII), we have
made the following improvements and new additions to enhance the
quality and overall functioning of the ProGlycProt V2.0 web-
resource.
466
Fig. 4. Statistics of ProGTdb. The percentage distribution of entries: (A) across phylum between (B) across domains (C) among N-, O- and S-glycosyltransferases
(D) according to mechanism of glycan transfer (E) depicting GT involved in sequential glycan transfer GT’s across various CAZy families (F) pathogenic and
non-pathogenic bacteria.
Creation of new web design and ProGlycProt V2.0 logo
The second release features a more user-friendly, mobile compat-
ible, easy to explore website where all the tools and search func-
tions are made available at homepage itself. The repository now
has a simple and self-explanatory logo to improve its web presence
and identity.
Rearrangement of ProGlycProt V2.0 ID to keep it
invariable in future updates
Entries in ProGlycProt V2.0, second release, are arranged chrono-
logically (criteria in the order of prioritization: year-month-date of
publication-genus-species-strain of the organism) to replace the
alphabetic listing assigned in the first version. The glycoproteins and
GTs/associated enzymes are cataloged independently (ProGP ID and
ProGT ID, respectively) yet cross-linked. Further, first release ID’s
P Choudhary et al.
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(AU101, AC101, etc.) have also been cited with revised ID’s to keep
it synchronized to the previous listing (Bhat et al. 2011).
Database model
The relationship between different data sets of ProGlycProt V2.0 is
represented as an Entity Relationship (ER) data model shown in
Figure 2. According to this entity model, each glycoprotein or glyco-
syltransferase is identified as either ProGP ID or ProGT ID, respect-
ively. Each ID provides manually curated information of organism/
gene/genome/protein/glycan/GT/literature, etc., and further externally
linked (dashed line arrow) to other protein/genome/organisms/struc-
tural identifier systems and reference databases (e.g., UniProt ID from
UniProt database). Data is organized into two sub-databases ProGTdb
(names in orange) and ProGPdb (names in yellow) containing several
meta tables tailored to allow efficient data mining and reduce process-
ing time by built-in functions. The individual table contains specific
ProGlycProt V2.0, a repository of glycoproteins and protein glycosyltransferases
information which is originally linked to its source table. Other entities
of the database like tools, search by features, the structural gallery are
shown in cyan color boxes which are interlinked to each other to
accommodate a given ProGP ID/ProGT ID.
Search by features
One of the ways to search and retrieve desired results from the
ProGlycProt V2.0 databases is by selecting search criteria among
four given choices namely, ProGP/GT ID, Organism, Protein Name,
UniProtKB/SwissProt ID and filtering the results by defining one of
the eleven given display criteria. In the second release, we provide
an additional option of search wherein user can search ProGTdb
and ProGPdb by scrolling down the menu and selecting one of the
classifying features namely, Organism, Gene, Donor, Protein,
Glycan, mechanism and Year. This leads to a quick overview of the
database entries sorted by the select classifier. The results are then
searchable and comparable by further ID selection steps (Figure 3).
Compare feature
This feature allows the user to compare as many as four different
selected ProGP or ProGT IDs directly or from the result display
page of any search function. This is particularly useful to compare
homologs (say of a given GT family) with respect to one (say
acceptor specificity) or more criteria. As the information load
increases, such features greatly enable filtering of useful information,
too.
ProGlycProt V2.0 MapView
A user-friendly new geoanalytical and location-assisted database
search tool is added at the home page that provides an interactive
view of all the laboratories/research groups corresponding to the
database entries in ProGlycProt V2.0, on a world map. Zoom out
function allows the user to explore information about the selected
entry(ies) in a location-specific manner. It also allows the user to
search or filter the entries on the map based on one or all of the fol-
lowing classifiers namely, organism name, subcellular location and
glycosylation type in a sub-database specific manner (ProGTdb/
ProGPdb). We believe, location assisted search is a very useful and
innovative feature for any academic database. This tool shall facili-
tate a quick overview of the spread of the expertise in this field and
quick identification of the labs to explore career and collaboration
opportunities for researchers/novice/curious minds, across the globe
or in a preferred location.
In second release all the ProGlycProt entries are cross-referred to
the most recent International glycan structure repository
GlyTouCan (Tiemeyer et al. 2017), in addition to already linked
BCSDB 3.0 (Herget et al. 2008), to benefit the users and to supple-
ment the structural information of the glycans (attached to proteins)
corresponding to a given entry.
User interface development
To facilitate better access to the information stored in the database,
we establish a user-friendly website. Each section is provided with
the example page and sufficient help tutorial at home page at the
help menu to ensure an easy use without any prerequisite knowledge
or experience. ProGlycProt V2.0 is developed by integrating the
data in MySQL, an open-source relational database management
system (RDBMS), which works at the backend, and the web inter-
face was built in PHP 5.4.0, HTML, CSS, JavaScript, jQuery and
467
Ajax. For the Map View functionality, the database system used is
PostgreSQL 9.5 and OpenStreetMap is employed for location dis-
play. Further, the client-side scripting of Map View is done using
JavaScript, jQuery, Underscore, Mustache, Data Driven Documents
and D3 Maps. The server-side scripting is done in Python 3.5.
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Supplementary data
Supplementary data is available at Glycobiology online.
Availability
ProGlycProt V2.0 is available freely at www.proglycprot.org
Note: The entire data pertaining to ProGlycProt, the first release is
archived and has been made available as downloadable file at the footer of
Home Page of ProGlycProt V2.0, second release under “Archive” button.
Funding
This work was supported by the ‘Council of Scientific and Industrial Research
[Grant numbers OLP0063, OLP0139 and MLP0021 to A.R.]’.
Acknowledgments
V.S., R.N., P.C., A.H.B. and Y.S. acknowledge the junior and senior research
fellowship awarded by CSIR/CSIR-UGC/DBT. We fondly and gratefully
acknowledge Showkat Ahmed Dar, Bioinformatics Centre, CSIR-Institute of
Microbial Technology, Chandigarh for his quick support and assistance in
setting up the BLAST tool.
Abbreviations
GT, glycosyltransferases; PTM, post-translational modification; eEF1A,
elongation factor 1 A; CAZy, carbohydrate-active enzymes; BLAST, basic local
alignment search tool; RDBMS, relational database management system; ProGP,
prokaryotic glycoproteins; ProGT, prokaryotic glycosyltransferase, BCSDB,
Bacterial Carbohydrate Structure DataBase.
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