The
DNA work on the Starchild Skull is now been prepared for peer
reviewed publication. This is described as an abstract but is much
of the paper itself.
Let
me make it simple.
The
Skull is Alien to Earth as we understand our DNA code. It may
possibly have been derived from Earth Stock through genetic
manipulation but I suspect that might be impossible. We do not know
enough yet to make such a determination.
The
individual lived long enough on Earth to establish a relationship and
to wear its teeth. Possibly for several years.
The
advanced skull suggests the application of nanotubes to artificially
strengthen the skull itself. This needs to be better investigated as
it may be applicable to adult humanity as bone will grow through and
around such a fiber net.
Regardless,
the genome represents the Rosseta Stone of human DNA by been a third
party comparable that allows us to sort out what is common and known
in a way that would otherwise be impossible.
Introduction. Around
1930, two skeletons were found in an abandoned mine tunnel in Mexico.
One was an apparently normal human, and the other was noticeably
shorter and misshapen. The skulls of both skeletons and a detached
piece of the broken upper jaw (maxilla) from the misshapen one
eventually ended up in a private collection in El Paso.
Over the past decade,
since 1999, both skulls were analyzed by dozens of scientists from
various areas of anthropology, none of whom disputed their
authenticity as human or human-like relics. Radiocarbon analysis
(C-14) indicated both individuals died around 900 years ago. There
are many morphological features that distinguish the misshapen skull
from a normal human skull, all of which point to significant
anatomical and physiological differences in the biological entity
from which the misshapen skull originated:
1. Bone of the
misshapen skull is less than one-third the thickness of the bone in a
human skull, and it weighs correspondingly less; (Fig. 2)
2. The misshapen
skull’s bone is much harder than human skull bone, as determined by
its strong resistance to cutting and drilling, which likely is a
consequence of biochemical differences and its internal architecture;
3. Its chemical makeup
resembles human tooth enamel much more than
the makeup of human
skeletal bone;
4. The misshapen skull
contained a brain of an apparently different shape (Fig. 3), which
was approximately 30% larger than normal human brains, as estimated
by measuring its cranial capacity;
5. Eye sockets of a
normal adult human are 1.5 – 2.0 inches deep, while the misshapen
skull’s eye sockets are barely 0.5 inch deep, which indicates the
corresponding biological entity had very different eyes;
6. As deduced from the
maxilla fragment, the entity’s mouth was infant-sized and had a
flat roof, with one of the arching that is normal in humans,
indicating either a very small or possibly missing tongue (Fig.4);
7. The maxilla
nevertheless shows a simultaneous presence of both wellworn adult
teeth and unerupted teeth visible in x-ray images (Fig.5);
8. CAT scan shows the
misshapen skull has much larger inner ears (Fig. 6).
Rationale. The skull’s
extremely unusual morphological features suggest that when death
occurred 900 years ago, it possessed anatomical and physiological
differences variant enough from normal humans to suggest it could
belong to an unknown humanoid species. However, morphological
evidence alone cannot substantiate the hypothesis.
A simple explanation
is that the entity was a human with a very rare disorder, or a
combination of disorders, that resulted in all of its observed
differences. This can be established if the individual’s genetic
makeup falls within the currently understood boundaries of human
genetic diversity. However, there must be a genetic basis forthe
development of such strong and durable bone, which on its own will
undoubtedly be of scientific, medical and practical significance. The
accumulated knowledge of the genetics of human bone formation will be
very helpful in the identification ofsimilarities and differences
between the genetic makeup of normal humans and the misshapen
individual.
On the farthest end of
the consideration range is the possibility that the entity was of
extraterrestrial origin in a general sense, and was not a part of, or
a result of, the evolution that connects all life forms on this
planet.
This scenario
represents an incomparably more challenging task, since most
techniques for studying life were developed using examples existing
on Earth. Did the entity use DNA, RNA and proteins to store and
utilize genetic information? How can one be confident even in the
possibility of collecting interpretable data? Our confidence is based
on a number of critical prerequisites. First and foremost, the
chemistry of the entity’s skull is similar to that of human bone.
Available elemental analysis demonstrated the presence of the same
elements as in human bone – carbon, oxygen, calcium, phosphate, and
others. Corroborating evidence is that the individual’s skull
displays worn teeth, perhaps from chewing gritty local foods,
implying that consumed food had at least some nutritional value and
was metabolically relevant.
However, the most
critical prerequisite for the collection of interpretable genetic
evidence is that the
biochemistry of the
entity must be similar to human biochemistry at the more complex
molecular and cellular levels. It must be based on the use of amino
acids, proteins, nucleotides, and nucleic acids (DNA and RNA).
Moreover, these
building blocks of life must be interconnected by a similarly
arranged flow of information and its encoding. Otherwise, the
molecular and genetic approaches developed for the analysis of
Earth’s existing life forms will be useless, similar to English
grammar being of virtually no value for understanding a Chinese text.
Recently, we obtained
molecular genetic evidence strongly indicating that this prerequisite
is also met.
The author of this
Abstract obtained skull bone samples under the condition that DNA
samples would be confined to one laboratory. DNA was extracted from
bone samples according to published protocols of ancient DNA
extraction, with all of the normal precautions taken against
contamination with modern DNA. It was then sequenced using a 454 GS
Jr instrument. Sequence reads of approximately 50 million nucleotides
in total length were compared with human genome sequences using the
accompanying software, and also analyzed by BLAST against the DNA
sequence database maintained by NCBI/NIH (GenBank). The majority of
reads did not match human sequences, or sequences of any species
deposited in the NCBI database. However, a substantial number of
reads did match human non-coding sequences, located in introns or
regulatory regions, or in so-called junk DNA, which together occupy >
90% of the human genome. Both of these findings were of low
informative value. However, one fragment has loosely matched exons 6
and 7 of the human FOXP2 gene. This fragment was analyzed further by
manually aligning it to the FOXP2 mRNA sequence of humans and several
other animals. The results of these multiple alignments are shown in
the Appendix, Fig. 1.
Human FOXP2 is known
as a “master switch” protein because it is produced very early in
the embryonic period to regulate over 300 other genes that are
responsible for the correct development of a human embryo. One of
FOXP2’s functions in humans is to control speech development, which
was acquired relatively recently in evolution, and separated humans
from the great apes.
All higher species
(mammals, birds, and fish) have species-specific variants of the
FOXP2 gene, which
despite certain
interspecies differences is still highly conserved due to its extreme
importance for embryonic development. In humans, the gene’s shown
fragment has only one synonymous difference (AG, indicated in the
human sequence by R, an IUPAC designation for puRine, either A or G)
found in the FOXP2 gene of a Wara South American Indian individual.
Twenty other human individuals belonging to different ethnicities and
language groups across the globe show exactly the same nucleotide
sequence in the corresponding fragment.
The chart in Appendix
1 shows the entity’s FOXP2-like fragment in comparison with matched
segments of FOXP2 from diverse animal species, from fish to humans.
While there are no variations at the protein level, except for
species-specific gaps or shortened variants, there are distinct
species-specific variations (depicted in red) in the protein coding
of corresponding DNA. This particular segment of FOXP2 is enriched in
glutamine(Gln), which is encoded in DNA by only two nucleotide
triplets, either CAG or CAA. Among other non-human species, only the
dog (a predator) displays six amino acid changes in this segment, all
clustered in one locus.
The rhesus macaque,
being quite distinct from humans, shows only one nucleotide
difference in this fragment (shown in red), with no amino acid
changes, and a deletion of exactly one triplet (one amino acid) as
compared to the human sequence.
Among the
211nucleotides of the entity’s FOXP2-like DNA fragment, we find a
stunning 62 differences t the nucleotide level, and 18 amino acid
differences (all shown in red). Apart from species-specific gaps,
this fragment shows more differences from the corresponding human
FOXP2 gene fragment than any species included in the comparison.
Moreover, the obtained sequence of the entity’s FOXP2-like DNA
fragment appears to represent a FOXP2-like pseudogene, since
sequences found in exons 6 and 7 of the human FOXP2 gene are
precisely spliced together in the entity’s genomic DNA. However, so
far no FOXP2 pseudogene is known to exist in humans or other
mammalian genomes. The stop codon interrupting the sequence shown in
blue) may or may not be present in the entity’s gene. It may result
from cytosine deamination known to occur in the DNA of ancient bones.
Such deamination results in the conversion of deoxycytidine to
deoxyuridine, which is recognized as deoxythymidine in a DNA
polymerase – a catalyzed reaction resulting in the observed CAGTAG
mutation. Due to the randomness of deamination events, such artifacts
can be accounted for by increasing the depth of coverage during
sequencing.
The probability that
such a highly specific arrangement of changes in a small fragment
could have occurred by accumulation of sequencing errors is extremely
low, if not close to zero. Nor could this arrangement have occurred
due to contamination with the DNA of any known species. From this
evidence one may conclude that the underlying biochemistry of the
entity’s life form must be either the same as, or highly similar
to, humans or other species. Yet, the use of the genetic code, which
still remains universal, is distinctively different, implying that
this life form is very likely the result of a markedly variant and
non-intersecting evolutionary process. This may be illustrated by
comparing Macintosh OS and Windows OS, both of which run on the same
Intel processor, or by comparing the grammar rules of English and
French, both of which belong to the same language group (Latin). The
most important point here is that in either case, despite the
existing differences, the encoded information can be recovered and
decoded.
We plan to approach
this challenge by identifying and analyzing the entity’s collagen
or collagen-like genes,which we believe should also constitute the
organic component of the entity’s bone. In all humans and other
mammals, collagen represents 25% to 35% of the body’s entire
protein content. Collagen fibrils are formed by packing two molecules
of collagen 1 and one molecule of collagen 2, which are encoded
by genes COL1A1 (Chr17) and COL1A2 (Chr7) in humans. The length of
the COL1A1gene is 17.54 kb with 51 exons, which after splicing is
translated to a precursor protein of 1464 amino acids. The length of
the COL1A2 gene is 36.67 kb with 52 exons that encode a precursor
protein of 1366 amino acids. Both proteins are enriched in Gly and
Pro(proline), with a characteristic repeat pattern of Gly-Xaa-Yaa.
In collagens, Gly is
highly conserved, since in fibrils formed by 1 and 2 chains it
is packed inside the triple helix with tight space constraints, which
disallow amino acids with side chains. Thus, one may expect that the
entity’s collagen or collagen-like proteins are arranged in a
similar way and contain conservative Gly. Exons coding for fragments
of these proteins can be identified by repeated GGN NNN NNN GG or GGN
NNN NNN GGN NNN NNN GG patterns, with a large number of NN in these
repeats being represented by CC.
As the entity’s
FOXP2-like fragment indicates, its genetic profile is based on the
use of the same universal genetic code, with Gly encoded by GGN
triples and Pro encoded by CCN triplets. Targeting conserved collagen
or collagen-like protein genes in the entity’s genome will enable
identification of exons and mapping of exonintron boundaries, thus
enabling definition of grammar and syntax of the unknown genetic
language. Decoding this information will enable reconstruction of
protein sequences encoded by corresponding genes, which then can be
assembled de novo and expressed in prokaryotic or eukaryotic hosts
for studies of their processing and biological properties. Since each
human collagen gene contains over 50 exons, deciphering the encoded
information can provide sufficient evidence for understanding how
different or similar is the molecular genetics of the life form
represented by the unknown biological entity, which will aid in
decoding other information stored within its genome.
We tested the
feasibility of this approach using the earlier collected sequencing
data set. Using rogram
FuzzNuc, a part of the
EMBOSS bioinfomatics package, we searched the obtained data set for a
pattern GGN(7)GGN(7)GGN(7)GGN(7)GG. Recovered hits were extracted
from the data set using their unique IDs,and translated into protein
using the universal genetic code. One of the fragments, shown in Fig.
2 in the Appendix, displayed the characteristic collagen coding
pattern – 21 Gly-Xaa-Yaa repeats highly enriched in proline (Pro).
Nucleotide and protein BLAST against the NCBI database indicated lack
of homology to human or mammalian sequences both at the nucleotide
and protein levels, indicating that the identified sequence is not
the result of contamination with human or animal DNA. However, the
fragment appeared loosely homologous to the 1 chains of human and
animal collagens of type VIII and type III. The fact that the
fragment encodes 21Gly-Xaa-Yaa repeats suggests that it actually
encodes a collagen VIII – like protein fragment. Genes of fibrillar
collagens (such as type I or III) contain about 50 exons, each of 54
bp in length (that is encoding 18 aa or six Gly-Xaa-Yaa repeats), or
occasionally 45 bp in length (five repeats). In contrast, the COL8A1
gene has only 5 exons, and only exons 4 and 5 encode long protein
fragments. As shown in Fig.2, the identified fragment indeed aligns
to a part of the longest exon 5 of the human COL8A1 gene. More
precise identification of this collagenlike protein requires
additional sequencing, but this example illustrates the feasibility
of the proposed approach.
General discussion of
other research in this area. DNA extraction from ancient bones has
been extensively studied and used for genetic characterization of
extinct animals and human relatives. This approach culminated in
recovery of the Neanderthal genome and discovery of the previously
unknown extinct relative of the Homo species, provisionally called
Denisova hominin. The existing instrumentation for next generation
sequencing technology includes genetic analyzers manufactured by
Illumina, Life Technologies (formerly Applied Biosystems) and 454
Life Sciences. Currently, the most widely used platform is Illumina,
which in a few days or a few weeks can produce from 5 Gb to 100 Gb of
sequence data, and it is supported by rapidly developing
bioinformatics tools. Since reliable sequence data require from 40X
to 100X coverage, an average mammalian genome of 3-5 Gb should be
sequenced many times over to cover all gaps and account for
inevitable errors and polymorphisms. We believe this task is well
within the limits and capabilities of modern molecular genetics.
Human collagens and
their genes are intensively studied both in basic and applied
biomedical research, in tissue bioengineering, and therapy of
injuries, such as wound healing. A vast body of literature, both
reviews and original publications, describe large numbers of assays
developed specifically for studies of the biological and biochemical
properties of collagens and their use in modern therapies. This
accumulated knowledge and expertise can be adapted to characterize
biological properties of novel collagens and collagen-like proteins
identified with the help of genetic studies proposed in this project.
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